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Entry version 103 (07 Oct 2020)
Sequence version 1 (11 Oct 2005)
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Protein

Hydrogenase maturation factor HypB

Gene

hypB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Involved in the maturation of [NiFe] hydrogenases. Required for nickel insertion into the metal center of the hydrogenase (PubMed:7601092, PubMed:8756471). Exhibits a low intrinsic GTPase activity, which is essential for nickel insertion (PubMed:7601092, PubMed:21544686, PubMed:27951644). In the presence of GDP, nickel, but not zinc, is transferred from the HypB GTPase domain (G-domain) to HypA (PubMed:23899293, PubMed:27951644).5 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Binding of zinc or nickel in the G-domain decreases GTPase activity (PubMed:21544686). Once GTP hydrolysis is triggered, probably via a GTPase activating protein, the GDP-loaded state may enhance HypA-HypB complex formation and reduces the affinity of HypB for nickel, which is then transferred to HypA (PubMed:27951644). In contrast to nickel, zinc reduces the formation of complexes with HypA (PubMed:27951644).2 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 0.18 min(-1) for GTPase activity. kcat is 0.04 min1 for GTPase activity in the presence of 1 µM Zn(II). kcat is 0.10 min(-1) for GTPase activity in the presence of 10 µM Ni(II).1 Publication

      Sites

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi2Nickel 12 Publications1
      Metal bindingi5Nickel 12 Publications1
      Metal bindingi7Nickel 12 Publications1
      Metal bindingi166Nickel 2 or zinc2 Publications1
      Metal bindingi167Nickel 2 or zinc2 Publications1
      Metal bindingi198Nickel 2 or zinc1 Publication1

      <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

      GO - Biological processi

      • protein maturation Source: EcoCyc

      <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

      Molecular functionHydrolase
      LigandGTP-binding, Metal-binding, Nickel, Nucleotide-binding, Zinc

      Enzyme and pathway databases

      BioCyc Collection of Pathway/Genome Databases

      More...
      BioCyci
      EcoCyc:EG10484-MONOMER
      MetaCyc:EG10484-MONOMER

      <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

      <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
      Recommended name:
      Hydrogenase maturation factor HypBCurated
      Alternative name(s):
      Hydrogenase isoenzymes nickel incorporation protein HypBCurated
      <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
      Name:hypB
      Ordered Locus Names:b2727, JW2697
      <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
      <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
      <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
      <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
      • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
      • UP000000625 Componenti: Chromosome

      <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

      Mutagenesis

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi2C → A: Decreases nickel content. Disruption of the N-terminal metal-binding site; when associated with A-5 and A-7. 1 Publication1
      Mutagenesisi5C → A: Decreases nickel content. Disruption of the N-terminal metal-binding site; when associated with A-3 and A-7. 1 Publication1
      Mutagenesisi7C → A: Decreases nickel content. Decreases hydrogenase activity of the cell. Disruption of the N-terminal metal-binding site; when associated with A-3 and A-5. 2 Publications1
      Mutagenesisi78 – 80LEV → AEA: Disrupts interaction with HypA. Can only partially restore hydrogenase production in a hypB deletion mutant. 1 Publication3
      Mutagenesisi117K → N: Important decrease in GTPase activity. 1 Publication1
      Mutagenesisi166C → A: Does not affect nickel content. Mutant lacks hydrogenase activity. 2 Publications1
      Mutagenesisi167H → A: Does not affect nickel content. Mutant lacks hydrogenase activity. 2 Publications1
      Mutagenesisi198C → A: Does not affect nickel content. 1 Publication1
      Mutagenesisi241D → N: 85-fold decrease in kcat/KM value of GTPase activity and loss of the specificity for GTP. 1 Publication1
      Mutagenesisi242L → A: Cannot form dimers. Can still bind metal in both sites and activate GTP hydrolysis, but hydrogenase activity of the cell is decreased; when associated with A-246. 1 Publication1
      Mutagenesisi246L → A: Cannot form dimers. Can still bind metal in both sites and activate GTP hydrolysis, but hydrogenase activity of the cell is decreased; when associated with A-242. 1 Publication1

      <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

      Molecule processing

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002014401 – 290Hydrogenase maturation factor HypBAdd BLAST290

      Proteomic databases

      jPOST - Japan Proteome Standard Repository/Database

      More...
      jPOSTi
      P0AAN3

      PaxDb, a database of protein abundance averages across all three domains of life

      More...
      PaxDbi
      P0AAN3

      PRoteomics IDEntifications database

      More...
      PRIDEi
      P0AAN3

      2D gel databases

      Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

      More...
      SWISS-2DPAGEi
      P0AAN3

      <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

      <p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

      Monomer (PubMed:21544686). Can form homodimers, but dimerization does not have a critical role in the hydrogenase maturation pathway (PubMed:21544686). Forms complexes with HypA and SlyD (PubMed:15995183, PubMed:15569666, PubMed:23899293).

      4 Publications

      <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

      Hide details

      Protein-protein interaction databases

      The Biological General Repository for Interaction Datasets (BioGRID)

      More...
      BioGRIDi
      4261427, 13 interactors

      ComplexPortal: manually curated resource of macromolecular complexes

      More...
      ComplexPortali
      CPX-5056, HypAB Ni-hydrogenase maturation complex

      Database of interacting proteins

      More...
      DIPi
      DIP-36428N

      Protein interaction database and analysis system

      More...
      IntActi
      P0AAN3, 9 interactors

      Molecular INTeraction database

      More...
      MINTi
      P0AAN3

      STRING: functional protein association networks

      More...
      STRINGi
      511145.b2727

      <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

      3D structure databases

      SWISS-MODEL Repository - a database of annotated 3D protein structure models

      More...
      SMRi
      P0AAN3

      Database of comparative protein structure models

      More...
      ModBasei
      Search...

      <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

      Region

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni106 – 267G-domainCuratedAdd BLAST162

      <p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

      The N-terminal region contains a high-affinity nickel-binding site and the C-terminal G-domain contains a low-affinity metal-binding site, which is not selective for nickel and could possibly accommodate other divalent metals (PubMed:16142921, PubMed:18942856). Both metal sites are critical for the maturation of the hydrogenases (PubMed:18942856).2 Publications

      <p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

      Phylogenomic databases

      evolutionary genealogy of genes: Non-supervised Orthologous Groups

      More...
      eggNOGi
      COG0378, Bacteria

      The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

      More...
      HOGENOMi
      CLU_056148_1_0_6

      InParanoid: Eukaryotic Ortholog Groups

      More...
      InParanoidi
      P0AAN3

      KEGG Orthology (KO)

      More...
      KOi
      K04652

      Database for complete collections of gene phylogenies

      More...
      PhylomeDBi
      P0AAN3

      Family and domain databases

      Conserved Domains Database

      More...
      CDDi
      cd05390, HypB, 1 hit

      Integrated resource of protein families, domains and functional sites

      More...
      InterProi
      View protein in InterPro
      IPR003495, CobW/HypB/UreG_dom
      IPR004392, Hyd_mat_HypB
      IPR027417, P-loop_NTPase

      The PANTHER Classification System

      More...
      PANTHERi
      PTHR30134, PTHR30134, 1 hit

      Pfam protein domain database

      More...
      Pfami
      View protein in Pfam
      PF02492, cobW, 1 hit

      Superfamily database of structural and functional annotation

      More...
      SUPFAMi
      SSF52540, SSF52540, 1 hit

      TIGRFAMs; a protein family database

      More...
      TIGRFAMsi
      TIGR00073, hypB, 1 hit

      <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

      <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

      P0AAN3-1 [UniParc]FASTAAdd to basket
      « Hide
              10         20         30         40         50
      MCTTCGCGEG NLYIEGDEHN PHSAFRSAPF APAARPKMKI TGIKAPEFTP
      60 70 80 90 100
      SQTEEGDLHY GHGEAGTHAP GMSQRRMLEV EIDVLDKNNR LAERNRARFA
      110 120 130 140 150
      ARKQLVLNLV SSPGSGKTTL LTETLMRLKD SVPCAVIEGD QQTVNDAARI
      160 170 180 190 200
      RATGTPAIQV NTGKGCHLDA QMIADAAPRL PLDDNGILFI ENVGNLVCPA
      210 220 230 240 250
      SFDLGEKHKV AVLSVTEGED KPLKYPHMFA AASLMLLNKV DLLPYLNFDV
      260 270 280 290
      EKCIACAREV NPEIEIILIS ATSGEGMDQW LNWLETQRCA
      Length:290
      Mass (Da):31,565
      Last modified:October 11, 2005 - v1
      <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i5B3AEB59AA6915C3
      GO

      Experimental Info

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti36P → R in CAA38413 (PubMed:1849603).Curated1

      Sequence databases

      Select the link destinations:

      EMBL nucleotide sequence database

      More...
      EMBLi

      GenBank nucleotide sequence database

      More...
      GenBanki

      DNA Data Bank of Japan; a nucleotide sequence database

      More...
      DDBJi
      Links Updated
      X54543 Genomic DNA Translation: CAA38413.1
      U29579 Genomic DNA Translation: AAA69237.1
      U00096 Genomic DNA Translation: AAC75769.1
      AP009048 Genomic DNA Translation: BAE76804.1

      Protein sequence database of the Protein Information Resource

      More...
      PIRi
      C65053

      NCBI Reference Sequences

      More...
      RefSeqi
      NP_417207.1, NC_000913.3
      WP_000337665.1, NZ_SSUR01000024.1

      Genome annotation databases

      Ensembl bacterial and archaeal genome annotation project

      More...
      EnsemblBacteriai
      AAC75769; AAC75769; b2727
      BAE76804; BAE76804; BAE76804

      Database of genes from NCBI RefSeq genomes

      More...
      GeneIDi
      48134403
      947194

      KEGG: Kyoto Encyclopedia of Genes and Genomes

      More...
      KEGGi
      ecj:JW2697
      eco:b2727

      Pathosystems Resource Integration Center (PATRIC)

      More...
      PATRICi
      fig|1411691.4.peg.4014

      <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

      Sequence databases

      Select the link destinations:
      EMBLi
      GenBanki
      DDBJi
      Links Updated
      X54543 Genomic DNA Translation: CAA38413.1
      U29579 Genomic DNA Translation: AAA69237.1
      U00096 Genomic DNA Translation: AAC75769.1
      AP009048 Genomic DNA Translation: BAE76804.1
      PIRiC65053
      RefSeqiNP_417207.1, NC_000913.3
      WP_000337665.1, NZ_SSUR01000024.1

      3D structure databases

      SMRiP0AAN3
      ModBaseiSearch...

      Protein-protein interaction databases

      BioGRIDi4261427, 13 interactors
      ComplexPortaliCPX-5056, HypAB Ni-hydrogenase maturation complex
      DIPiDIP-36428N
      IntActiP0AAN3, 9 interactors
      MINTiP0AAN3
      STRINGi511145.b2727

      2D gel databases

      SWISS-2DPAGEiP0AAN3

      Proteomic databases

      jPOSTiP0AAN3
      PaxDbiP0AAN3
      PRIDEiP0AAN3

      Genome annotation databases

      EnsemblBacteriaiAAC75769; AAC75769; b2727
      BAE76804; BAE76804; BAE76804
      GeneIDi48134403
      947194
      KEGGiecj:JW2697
      eco:b2727
      PATRICifig|1411691.4.peg.4014

      Organism-specific databases

      EchoBASE - an integrated post-genomic database for E. coli

      More...
      EchoBASEi
      EB0479

      Phylogenomic databases

      eggNOGiCOG0378, Bacteria
      HOGENOMiCLU_056148_1_0_6
      InParanoidiP0AAN3
      KOiK04652
      PhylomeDBiP0AAN3

      Enzyme and pathway databases

      BioCyciEcoCyc:EG10484-MONOMER
      MetaCyc:EG10484-MONOMER

      Miscellaneous databases

      Protein Ontology

      More...
      PROi
      PR:P0AAN3

      Family and domain databases

      CDDicd05390, HypB, 1 hit
      InterProiView protein in InterPro
      IPR003495, CobW/HypB/UreG_dom
      IPR004392, Hyd_mat_HypB
      IPR027417, P-loop_NTPase
      PANTHERiPTHR30134, PTHR30134, 1 hit
      PfamiView protein in Pfam
      PF02492, cobW, 1 hit
      SUPFAMiSSF52540, SSF52540, 1 hit
      TIGRFAMsiTIGR00073, hypB, 1 hit

      ProtoNet; Automatic hierarchical classification of proteins

      More...
      ProtoNeti
      Search...

      MobiDB: a database of protein disorder and mobility annotations

      More...
      MobiDBi
      Search...

      <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

      <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiHYPB_ECOLI
      <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P0AAN3
      Secondary accession number(s): P24190, Q2MAA2, Q46884
      <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 11, 2005
      Last sequence update: October 11, 2005
      Last modified: October 7, 2020
      This is version 103 of the entry and version 1 of the sequence. See complete history.
      <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
      Annotation programProkaryotic Protein Annotation Program

      <p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

      Keywords - Technical termi

      Direct protein sequencing, Reference proteome

      Documents

      1. Escherichia coli
        Escherichia coli (strain K12): entries and cross-references to EcoGene
      2. SIMILARITY comments
        Index of protein domains and families
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