NEAT: a domain duplicated in genes near the components of a putative Fe3+siderophore transporter from Gram-positive pathogenic bacteria

Andrade, Miguel A; Ciccarelli, Francesca D; Perez-Iratxeta, Carolina; Bork, Peer

doi:10.1186/gb-2002-3-9-research0047

Cited by 135Bacterial Genetics and BiotechnologyIron Metabolism and DisordersGenomics and Phylogenetic Studies

NEAT: a domain duplicated in genes near the components of a putative Fe3+siderophore transporter from Gram-positive pathogenic bacteria

Open access

Andrade, Miguel A, Ciccarelli, Francesca D, Perez-Iratxeta, Carolina, Bork, Peer·2002·Genome Biology

DOI 10.1186/gb-2002-3-9-research0047PMC PMC126872

Open this paper in CoChat — free account Open PDF

Abstract

BACKGROUND: Iron uptake from the host is essential for bacteria that infect animals. To find potential targets for drugs active against pathogenic bacteria, we have searched all completely sequenced genomes of pathogenic bacteria for genes relevant for iron transport. RESULTS: We identified a protein domain that appears in variable copy number in bacterial genes that are usually in the vicinity of a putative Fe3+ siderophore transporter. Accordingly, we have denoted this domain NEAT for 'near transporter'. Most of the bacterial species containing this domain are pathogenic. Sequence features indicate that the domain is anchored to the extracellular side of the membrane. The domain seems to be under high selective pressure for rapid independent duplications that are typical of sequences involved in signaling and binding. CONCLUSIONS: The NEAT domain might be functionally related to iron transport. The taxonomic specificity of this domain and its predicted extracellular position could make it an interesting target for designing new drugs against some highly pathogenic bacteria.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1186/gb-2002-3-9-research0047

Cites

30 of 30 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

NEAT domains are conserved 125-amino-acid stretches found in proteins that neighbor putative iron transporters.
“NEAT domains are conserved stretches of 125 amino acids found within proteins that neighbor putative iron transporters (2).”
From Molecular Mechanisms of Staphylococcus aureus Iron Acquisition (2011) · cites this paper as [2]

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
Thompson, J. D., Higgins, D. G., & Gibson, T. J. (1994) · Nucleic Acids Research · doi:10.1093/nar/22.22.4673 · Cited by 64,617 · see citing works
The Pfam Protein Families Database
Bateman, A. G. (2002) · Nucleic Acids Research · doi:10.1093/nar/30.1.276 · Cited by 14,062 · see citing works
Predicting transmembrane protein topology with a hidden markov model: application to complete genomes11Edited by F. Cohen
Krogh, A., Larsson, B., von Heijne, G., & Sonnhammer, E. L. L. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.4315 · Cited by 12,654 · see citing works
Profile hidden Markov models
Eddy, S. R. (1998) · Bioinformatics · doi:10.1093/bioinformatics/14.9.755 · Cited by 5,515 · see citing works
A new method for predicting signal sequence cleavage sites
von HEIJNE, G. (1986) · Nucleic Acids Research · doi:10.1093/nar/14.11.4683 · Cited by 4,554 · see citing works
SMART, a simple modular architecture research tool: Identification of signaling domains
Schultz, J., Milpetz, F., Peer Bork, B., & Ponting, C. P. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.5857 · Cited by 3,577 · see citing works
Whole genome sequencing of meticillin-resistant Staphylococcus aureus
Kuroda, M., Ohta, T., Uchiyama, I., Baba, T., Yuzawa, H., Kobayashi, I., Cui, L., Oguchi, A., Aoki, K.-I., Nagai, Y., et al. (2001) · The Lancet · doi:10.1016/s0140-6736(00)04403-2 · Cited by 1,950 · see citing works
Iron Metabolism in Pathogenic Bacteria
Ratledge, C., & Dover, L. G. (2000) · Annual Review of Microbiology · doi:10.1146/annurev.micro.54.1.881 · Cited by 1,539 · see citing works
Comparative Genomics of Listeria Species
Glaser, P., Frangeul, L., Buchrieser, C., Rusniok, C., Amend, A., Baquero, F., Berche, P., Blöcker, H., Brandt, P., Chakraborty, T., et al. (2001) · Science · doi:10.1126/science.1063447 · Cited by 1,505 · see citing works
Combining evolutionary information and neural networks to predict protein secondary structure
Rost, B., & Sander, C. (1994) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340190108 · Cited by 1,452 · see citing works
The use of gene clusters to infer functional coupling.
Overbeek, R., Fonstein, M., D'Souza, M., Pusch, G., & Maltsev, N. (1999) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.96.6.2896 · Cited by 1,365 · see citing works
STRING: a web-server to retrieve and display the repeatedly occurring neighbourhood of a gene
Snel, ‎. (2000) · Nucleic Acids Research · doi:10.1093/nar/28.18.3442 · Cited by 1,240 · see citing works
Conservation of gene order: a fingerprint of proteins that physically interact.
Dandekar, T., Snel, B., Huynen, M., & Bork, P. (1998) · TIBS -Trends in Biochemical Sciences. Regular ed · doi:10.1016/s0968-0004(98)01274-2 · Cited by 1,108 · see citing works
Self-citation
Complete genome sequence of an M1 strain of Streptococcus pyogenes
Ferretti, J. J., McShan, W. M., Ajdić, D., Savić, D. J., Savić, G., Lyon, K., Primeaux, C., Sezate, S. A., Suvorov, A. N., Kenton, S., et al. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.071559398 · Cited by 936 · see citing works
The Pfam Protein Families Database
Bateman, A. G., Birney, E., Cerruti, L., Durbin, R. M., Etwiller, L., Eddy, S. R., Griffiths‐Jones, S., Howe, K., Marshall, M. S., & Sonnhammer, E. L. L. (2002) · PubMed Central · Cited by 764 · see citing works
Complete genome sequence of Clostridium perfringens , an anaerobic flesh-eater
Shimizu, T., Ohtani, K., Hirakawa, H., Ohshima, K., Yamashita, A., Shiba, T., Ogasawara, N., Hattori, M., Kuhara, S., & Hayashi, H. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.022493799 · Cited by 726 · see citing works
Recent improvements to the SMART domain-based sequence annotation resource
Letunić, I. (2002) · Nucleic Acids Research · doi:10.1093/nar/30.1.242 · Cited by 679 · see citing works
Protein Repeats: Structures, Functions, and Evolution
Andrade-Navarro, M. A., Perez‐Iratxeta, C., & Ponting, C. P. (2001) · Journal of Structural Biology · doi:10.1006/jsbi.2001.4392 · Cited by 613 · see citing works
Self-citation
Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis
Takami, H. (2000) · Nucleic Acids Research · doi:10.1093/nar/28.21.4317 · Cited by 528 · see citing works
Conservation of a hexapeptide sequence in the anchor region of surface proteins from Gram‐positive cocci
Fischetti, V. A., Pancholi, V., & Schneewind, O. (1990) · Molecular Microbiology · doi:10.1111/j.1365-2958.1990.tb02072.x · Cited by 411 · see citing works
Sequence and Organization of pXO1, the Large Bacillus anthracis Plasmid Harboring the Anthrax Toxin Genes
Okinaka, R. T., Cloud, K. G., Hampton, O. A., Hoffmaster, A. R., Hill, K. K., Keim, P., Koehler, T. M., Lamke, G., Kumano, S., Mahillon, J., et al. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.20.6509-6515.1999 · Cited by 390 · see citing works
Nucleotide sequences of the fecBCDE genes and locations of the proteins suggest a periplasmic-binding-protein-dependent transport mechanism for iron(III) dicitrate in Escherichia coli
Staudenmaier, H., Hove, B. V., Yaraghi, Z., & Braun, V. (1989) · Journal of Bacteriology · doi:10.1128/jb.171.5.2626-2633.1989 · Cited by 209 · see citing works
Homology-based method for identification of protein repeats using statistical significance estimates
Andrade-Navarro, M. A., Ponting, C. P., Gibson, T. J., et al. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3684 · Cited by 188 · see citing works
Surface Signaling in Ferric Citrate Transport Gene Induction: Interaction of the FecA, FecR, and FecI Regulatory Proteins
Enz, S., Mahren, S., Stroeher, U. H., & Braun, V. (2000) · Journal of Bacteriology · doi:10.1128/jb.182.3.637-646.2000 · Cited by 126 · see citing works
Accurate formula for P-values of gapped local sequence and profile alignments
Mott, R. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3875 · Cited by 117 · see citing works
Genetic organization of multiple fep genes encoding ferric enterobactin transport functions in Escherichia coli
Ozenberger, B. A., Nahlik, M. S., & McIntosh, M. A. (1987) · Journal of Bacteriology · doi:10.1128/jb.169.8.3638-3646.1987 · Cited by 91 · see citing works
Exploitation of gene context
Huynen, M. A., Snel, ‎., Lathe, W. C., et al. (2000) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(00)00098-1 · Cited by 85 · see citing works
SMART, a simple modular architecture research tool
Schultz, J., Milpetz, F., Peer Bork, B., et al. (1998) · Proceedings of the National Academy of Sciences · Cited by 62 · see citing works
Nucleotide sequence of the fhuC and fhuD genes involved in iron (III) hydroxamate transport: Domains in FhuC homologous to ATP-binding proteins
Burkhardt, R., & Braun, V. (1987) · Molecular and General Genetics MGG · doi:10.1007/bf00329835 · Cited by 61 · see citing works
Conservation, Surface Exposure, and In Vivo Expression of the Frp Family of Iron-Regulated Cell Wall Proteins in Staphylococcus aureus
Morrissey, J. A., Cockayne, A., Hammacott, J. E., Bishop, K., Denman-Johnson, A., Hill, P. J., & Williams, P. M. (2002) · Infection and Immunity · doi:10.1128/iai.70.5.2399-2407.2002 · Cited by 49 · see citing works

Flagged first, then by citations

Sorted by citations

Molecular Mechanisms of Staphylococcus aureus Iron Acquisition
Hammer, N. D., & Skaar, E. P. (2011) · Annual Review of Microbiology · doi:10.1146/annurev-micro-090110-102851 · Cited by 379 · see citing works
Shared and distinct mechanisms of iron acquisition by bacterial and fungal pathogens of humans
Caza, M., & Kronstad, J. W. (2013) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2013.00080 · Cited by 306 · see citing works
A Novel Staphylococcus aureus Vaccine: Iron Surface Determinant B Induces Rapid Antibody Responses in Rhesus Macaques and Specific Increased Survival in a Murine S. aureus Sepsis Model
Kuklin, N. A., Clark, D. J., Secore, S., Cook, J., Cope, L. D., McNeely, T., Noble, L., Brown, M. J., Zorman, J. K., Wang, X. M., et al. (2006) · Infection and Immunity · doi:10.1128/iai.74.4.2215-2223.2006 · Cited by 264 · see citing works
Sequestration and scavenging of iron in infection
Parrow, N. L., Fleming, R. E., & Minnick, M. F. (2013) · Infection and Immunity · doi:10.1128/iai.00602-13 · Cited by 261 · see citing works
Iron acquisition strategies of bacterial pathogens
Sheldon, J. R., Laakso, H. A., & Heinrichs, D. E. (2016) · Microbiology Spectrum · doi:10.1128/microbiolspec.vmbf-0010-2015 · Cited by 219 · see citing works
A Comparative Genome Analysis Identifies Distinct Sorting Pathways in Gram-Positive Bacteria
Comfort, D., & Clubb, R. T. (2004) · Infection and Immunity · doi:10.1128/iai.72.5.2710-2722.2004 · Cited by 203 · see citing works
Haem recognition by a Staphylococcus aureus NEAT domain
Grigg, J. C., Vermeiren, C. L., Heinrichs, D. E., & Murphy, M. E. P. (2007) · Molecular Microbiology · doi:10.1111/j.1365-2958.2006.05502.x · Cited by 166 · see citing works
IsdA of Staphylococcus aureus is a broad spectrum, iron‐regulated adhesin
Clarke, S. R., Wiltshire, M. D., & Foster, S. J. (2004) · Molecular Microbiology · doi:10.1111/j.1365-2958.2003.03938.x · Cited by 150 · see citing works
Bacillus anthracis secretes proteins that mediate heme acquisition from hemoglobin
Maresso, A. W., Garufi, G., & Schneewind, O. (2008) · PLoS Pathogens · doi:10.1371/journal.ppat.1000132 · Cited by 144 · see citing works
Surface Protein IsdC and Sortase B Are Required for Heme-Iron Scavenging ofBacillus anthracis
Maresso, A. W., Chapa, T. J., & Schneewind, O. (2006) · Journal of Bacteriology · doi:10.1128/jb.01011-06 · Cited by 135 · see citing works
Pathway for Heme Uptake from Human Methemoglobin by the Iron-regulated Surface Determinants System of Staphylococcus aureus
Zhu, H., Xie, G., Liu, M., Olson, J. S., Fabian, M., Dooley, D. M., & Lei, B. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801466200 · Cited by 127 · see citing works
Direct Hemin Transfer from IsdA to IsdC in the Iron-regulated Surface Determinant (Isd) Heme Acquisition System of Staphylococcus aureus
Liu, M., Tanaka, W. N., Zhu, H., Xie, G., Dooley, D. M., & Lei, B. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m708372200 · Cited by 129 · see citing works
Functionally distinct NEAT (NEAr Transporter) domains within the Staphylococcus aureus IsdH/HarA protein extract heme from methemoglobin
Pilpa, R. M., Robson, S. A., Villareal, V. A., Wong, M. L., Phillips, M., & Clubb, R. T. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m806007200 · Cited by 118 · see citing works
Iron-Regulated Surface Determinant Protein A Mediates Adhesion ofStaphylococcus aureusto Human Corneocyte Envelope Proteins
Clarke, S. R., Andre, G., Walsh, E. J., Dufrêne, Y. F., Foster, T. J., & Foster, S. J. (2009) · Infection and Immunity · doi:10.1128/iai.01304-08 · Cited by 105 · see citing works
Shr is a broad-spectrum surface receptor that contributes to adherence and virulence in group A streptococcus.
Fisher, M., Huang, Y.-S., Li, X., McIver, K. S., Toukoki, C., & Eichenbaum, Z. (2008) · Infection and Immunity · doi:10.1128/iai.00300-08 · Cited by 90 · see citing works
The surface protein Shr of Streptococcus pyogenes binds heme and transfers it to the streptococcal heme-binding protein Shp.
Zhu, H., Liu, M., & Lei, B. (2008) · BMC Microbiology · doi:10.1186/1471-2180-8-15 · Cited by 82 · see citing works
Staphylococcus aureus heme and siderophore-iron acquisition pathways
Conroy, B. S., Grigg, J. C., Kolesnikov, M., Morales, L. D., & Murphy, M. E. P. (2019) · BioMetals · doi:10.1007/s10534-019-00188-2 · Cited by 73 · see citing works
ABacillus anthracisS-Layer Homology Protein That Binds Heme and Mediates Heme Delivery to IsdC
Tarlovsky, Y., Fabian, M., Solomaha, E., Honsa, E., Olson, J. S., & Maresso, A. W. (2010) · Journal of Bacteriology · doi:10.1128/jb.00054-10 · Cited by 72 · see citing works
Immune evasion by Staphylococcus aureus conferred by iron-regulated surface determinant protein IsdH
Visai, L., Yanagisawa, N., Josefsson, E., Tarkowski, A., Pezzali, I., Rooijakkers, S. H. M., Foster, T. J., & Speziale, P. (2009) · Microbiology · doi:10.1099/mic.0.025684-0 · Cited by 73 · see citing works
High-Affinity Binding of the Staphylococcal HarA Protein to Haptoglobin and Hemoglobin Involves a Domain with an Antiparallel Eight-Stranded β-Barrel Fold
Dryla, A., Hoffmann, B., Gelbmann, D., Giefing, C., Hanner, M., Meinke, A., Anderson, A. S., Koppensteiner, W., Konrat, R., von Gabain, A., et al. (2007) · Journal of Bacteriology · doi:10.1128/jb.01366-06 · Cited by 73 · see citing works
Shr of group A streptococcus is a new type of composite NEAT protein involved in sequestering haem from methaemoglobin
Ouattara, M., Bentley Cunha, E., Li, X., Huang, Y., Dixon, D., & Eichenbaum, Z. (2010) · Molecular Microbiology · doi:10.1111/j.1365-2958.2010.07367.x · Cited by 71 · see citing works
Heme transfer to the bacterial cell envelope occurs via a secreted hemophore in the Gram-positive pathogen Bacillus anthracis
Fabian, M., Solomaha, E., Olson, J. S., & Maresso, A. W. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.040915 · Cited by 70 · see citing works
Characterization of Bacillus anthracis iron‐regulated surface determinant (Isd) proteins containing NEAT domains
Gat, O., Zaide, G., Inbar, I., Grosfeld, H., Chitlaru, T., Levy, H., & Shafferman, A. (2008) · Molecular Microbiology · doi:10.1111/j.1365-2958.2008.06460.x · Cited by 68 · see citing works
The five near-iron transporter (NEAT) domain anthrax hemophore, IsdX2, scavenges heme from hemoglobin and transfers heme to the surface protein IsdC
Honsa, E. S., Fabian, M., Cardenas, A. M., Olson, J. S., & Maresso, A. W. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.241687 · Cited by 50 · see citing works
Novel hemin binding domains in the Corynebacterium diphtheriae HtaA protein interact with hemoglobin and are critical for heme iron utilization by HtaA
Allen, C. E., & Schmitt, M. P. (2011) · Journal of Bacteriology · doi:10.1128/jb.05508-11 · Cited by 46 · see citing works
Utilization of host iron sources by Corynebacterium diphtheriae: multiple hemoglobin-binding proteins are essential for the use of iron from the hemoglobin–haptoglobin complex
Allen, C. E., & Schmitt, M. P. (2015) · Journal of Bacteriology · doi:10.1128/jb.02413-14 · Cited by 44 · see citing works
Analysis of novel iron-regulated, surface-anchored hemin-binding proteins in Corynebacterium diphtheriae
Allen, C. E., Burgos, J. M., & Schmitt, M. P. (2013) · Journal of Bacteriology · doi:10.1128/jb.00244-13 · Cited by 35 · see citing works
Solution Structure and Molecular Determinants of Hemoglobin Binding of the First NEAT Domain of IsdB in Staphylococcus aureus
Fonner, B. A., Tripet, B. P., Eilers, B. J., Stanisich, J., Sullivan-Springhetti, R. K., Moore, R., Liu, M., Lei, B., & Copié, V. (2014) · Biochemistry · doi:10.1021/bi5005188 · Cited by 31 · see citing works
The human protein haptoglobin inhibits IsdH-mediated heme-sequestering by Staphylococcus aureus
Mikkelsen, J. H., Runager, K., & Andersen, C. B. F. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.011612 · Cited by 27 · see citing works
Heme Binding by Corynebacterium diphtheriae HmuT: Function and Heme Environment
Draganova, E. B., Akbas, N., Adrian, S. A., Lukat-Rodgers, G. S., Collins, D. P., Dawson, J. H., Allen, C. E., Schmitt, M. P., Rodgers, K. R., & Dixon, D. W. (2015) · Biochemistry · doi:10.1021/acs.biochem.5b00666 · Cited by 26 · see citing works
The near-iron transporter (NEAT) domains of the anthrax hemophore IsdX2 require a critical glutamine to extract heme from methemoglobin
Honsa, E. S., Owens, C. P., Goulding, C. W., & Maresso, A. W. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.430009 · Cited by 28 · see citing works
Kinetics of heme transfer by the Shr NEAT domains of Group A Streptococcus
Ouattara, M., Pennati, A., Devlin, D. J., Huang, Y.-S., Gadda, G., & Eichenbaum, Z. (2013) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2013.08.009 · Cited by 26 · see citing works
Iron Acquisition Strategies of Bacterial Pathogens
Sheldon, J. R., Laakso, H. A., & Heinrichs, D. E. (2016) · Virulence Mechanisms of Bacterial Pathogens · doi:10.1128/9781555819286.ch3 · Cited by 25 · see citing works
The streptococcal hemoprotein receptor: A moonlighting protein or a virulence factor?
Eichenbaum, Z. (2012) · Virulence · doi:10.4161/viru.22440 · Cited by 8 · see citing works

Inactivation of siderophore iron‐chelating moieties by the fungal wheat root symbiont Pyrenophora biseptata
French, K. S., Chukwuma, E., Linshitz, I., Namba, K., Duckworth, O. W., Cubeta, M. A., & Baars, O. (2024) · Environmental Microbiology Reports · doi:10.1111/1758-2229.13234 · Cited by 9 · see citing works
Characterization of Siderophore Producing Rhizobacteria and its Effect on Growth of Pea
Nazir, U., & Zargar, M. Y. (2023) · International Journal of Current Microbiology and Applied Sciences · doi:10.20546/ijcmas.2023.1201.017
Effect of Exogenous Siderophores on Iron Uptake Activity of Marine Bacteria under Iron-Limited Conditions
Guan, L. L., Kanoh, K., & Kamino, K. (2001) · Applied and Environmental Microbiology · doi:10.1128/aem.67.4.1710-1717.2001 · Cited by 102 · see citing works
Detection and chemical characterisation of siderophores of rhizobacterial Fluorescent Pseudomonas
Dave, B. P., & Dube, H. C. (2000) · Indian Phytopathology · Cited by 13 · see citing works
SIDEROPHORE PRODUCTION BY THE ISOLATES OF FLUORESCENT PSEUDOMONADS
Sujatha, N., & Ammani, K. (2013) · International Journal of Current Research and Review · Cited by 39 · see citing works

Authors: Andrade, M. A., Ciccarelli, F. D., Perez-Iratxeta, C., & Bork, P.
Affiliations: Max Delbrück Center (DE)
ORCID: Ciccarelli, Francesca D
Venue: Genome Biology
Publisher: Springer Science and Business Media LLC
Published: 2002-08-15
Volume: 3
Issue: 9
Pages: RESEARCH0047-RESEARCH0047
ISSN: 1465-6906 (ISSN-L)
1474-760X
DOI: 10.1186/gb-2002-3-9-research0047
PMC: PMC126872
OpenAlex: W2097664182
Cited by: 135
References: 30
Citations by year: 2026: 1 · 2025: 3 · 2024: 1 · 2023: 3 · 2022: 7 · 2021: 4 · 2020: 4 · 2019: 5 · 2018: 4 · 2017: 4 · 2016: 10 · 2015: 6 · 2014: 10 · 2013: 9 · 2012: 9
FWCI: 1.41
Type: journal article
Language: en
Open access: gold
doi.org
Licence: www.springernature.com/gp/researchers/text-and-data-mining (tdm)
www.springernature.com/gp/researchers/text-and-data-mining (vor)
Locations: Genome biology (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Research Portal (King's College London) (publishedVersion, other-oa)
MDC Repository (Max-Delbrueck-Center for Molecular Medicine) (acceptedVersion)
Archivio Istituzionale della Ricerca (Universita Degli Studi Di Milano) (submittedVersion, cc-by-sa)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Phylogenetic Studies
Keywords: NEAT domain, iron transport, siderophore transporters, gene duplication, therapeutic target, host-pathogen interaction, selection pressure, bacterial genomes
MeSH terms: Amino Acid Sequence, Bacterial Proteins, Binding Sites, Carrier Proteins, Ferric Compounds, Gram-Positive Bacteria, Molecular Sequence Data, Phylogeny, Sequence Alignment, Genome, Bacterial, Siderophores, Sequence Homology, Amino Acid, Gene Duplication

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

NEAT: a domain duplicated in genes near the components of a putative Fe3+siderophore transporter from Gram-positive pathogenic bacteria

Abstract

Integrity signals

Claims the paper makes

Claims other papers make about this one

Self-check

Cites

Cited by

Related

Record

About these checks