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Entry version 111 (11 Dec 2019)
Sequence version 1 (01 Feb 1994)
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Protein

Stage IV sporulation protein A

Gene

spoIVA

Organism
Bacillus subtilis (strain 168)
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

ATPase. Has a role at an early stage in the morphogenesis of the spore coat outer layers. Its ATP hydrolysis is required for proper assembly of the spore coat. Forms a basement layer around the outside surface of the forespore and self-assembles irreversibly into higher order structures by binding and hydrolyzing ATP thus creating a durable and stable platform upon which thereafter morphogenesis of the coat can take place. Required for proper localization of spore coat protein CotE and sporulation-specific proteins including SpoVM.5 Publications

Miscellaneous

Present in an increased level in yabG mutant spores.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<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

The turnover rate is 2.7 pmol/min/pmol of SpoIVA at Vmax (PubMed:18691972). The turnover rate is 1.0 pmol/min/pmol of SpoIVA at Vmax (PubMed:23267091).2 Publications
  1. KM=412 µM for ATP2 Publications

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi24 – 31ATPCurated8

    <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

    <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
    Biological processSporulation
    LigandATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    BSUB:BSU22800-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_and_taxonomy_section">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:
    Stage IV sporulation protein A (EC:3.6.1.3)
    Alternative name(s):
    Coat morphogenetic protein SpoIVA
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:spoIVA
    Synonyms:spoVP
    Ordered Locus Names:BSU22800
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiBacillus subtilis (strain 168)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri224308 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
    • UP000001570 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    GO - Cellular componenti

    Keywords - Cellular componenti

    Cytoplasm

    <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

    <p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

    Forespores lack a well-defined cortex, and the coat is present as swirls in the mother cell compartment of the sporangia rather than having been deposited around the forespore protoplasts. According to PubMed:18691972, unable to sporulate.3 Publications

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi30K → A: 20-fold reduction in sporulation efficiency. Largely enriched at the forespore periphery, although some localization to the cytosol. Binding of ATP reduced over 23-fold. Leads to diminished ATP hydrolysis. 1 Publication1
    Mutagenesisi30K → E: Mislocalized to the mother cell cytosol. Misassembles the spore coat. Mislocalizes CotE but not SpoVM. Does not multimerize. Almost complete block in spore formation. 1 Publication1
    Mutagenesisi59L → P: Spores form largely normal coats and possess at least some cortex, but cannot remain dehydrated after mother cell lysis. Abnormal synthesis and an insufficient level of spore peptidoglycan, which contains amidated diaminopimelic acid, which is normally found only in vegetative cell peptidoglycan. Defective in germination; when associated with P-256. 1 Publication1
    Mutagenesisi69M → L: Altered cortex and coat formation; when associated with S-230. 1 Publication1
    Mutagenesisi70T → A: 500-fold decrease in sporulation efficiency. 5-log decrease in sporulation efficiency; no ATPase activity, but no change in ATP-binding ability; unable to polymerize and fails to promote coat assembly; when associated with A-71. 1 Publication1
    Mutagenesisi71T → A: Does not abrogate sporulation. 5-log decrease in sporulation efficiency; no ATPase activity, but no change in ATP-binding ability; unable to polymerize and fails to promote coat assembly; when associated with A-70. 1 Publication1
    Mutagenesisi97D → A: Completely abolished sporulation efficiency. No ATPase activity, but no change in ATP-binding ability. Unable to polymerize and fails to promote coat assembly;. 1 Publication1
    Mutagenesisi98C → S: Defective in germination; when associated with N-283. 1 Publication1
    Mutagenesisi189S → K: Unable to sporulate. 1 Publication1
    Mutagenesisi210I → A: Defective in germination; when associated with V-367 and R-383. 1 Publication1
    Mutagenesisi210I → M: Altered cortex and coat formation; when associated with V-367 and R-383. 1 Publication1
    Mutagenesisi230R → S: Altered cortex and coat formation; when associated with L-69. 1 Publication1
    Mutagenesisi241V → G: Altered cortex and coat formation. 1 Publication1
    Mutagenesisi256H → P: Defective in germination; when associated with P-59. 1 Publication1
    Mutagenesisi283V → N: Defective in germination; when associated with S-98. 1 Publication1
    Mutagenesisi367I → V: Defective in germination; when associated with A-210 and R-383. Altered cortex and coat formation; when associated with M-210 and R-383. 1 Publication1
    Mutagenesisi383I → R: Defective in germination; when associated with A-210 and V-367. Altered cortex and coat formation; when associated with M-210 and R-383. 1 Publication1
    Mutagenesisi393L → P: Altered cortex and coat formation. Possesses swirls of coat in the mother cell cytoplasm and does not possess a cortex. 1 Publication1
    Mutagenesisi400I → P: Altered cortex and coat formation, affects localization to the forespore; when associated with R-457 and V-418. 1 Publication1
    Mutagenesisi416G → R: Altered cortex and coat formation. 1 Publication1
    Mutagenesisi418E → V: Altered cortex and coat formation, affects localization to the forespore; when associated with P-400 and R-457. 1 Publication1
    Mutagenesisi453V → G: Altered cortex and coat formation, affects localization to the forespore. 1 Publication1
    Mutagenesisi457I → R: Altered cortex and coat formation, affects localization to the forespore; when associated with P-400 and V-418. 1 Publication1
    Mutagenesisi486G → V: Suppressor mutation that reverses the mislocalization and sporulation defect of the A-6 mutation in SpoVM. Causes little impairment of sporulation. 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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000720731 – 492Stage IV sporulation protein AAdd BLAST492

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

    Seems to be cleaved by the YabG protease.1 Publication

    Proteomic databases

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

    More...
    PaxDbi
    P35149

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P35149

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

    Expressed soon after the formation of the asymmetric septum during sporulation. Expression commences about 2 hours after the onset of sporulation. Assembly around the developing forespore commences at the time of polar division and seems to continue after engulfment of the forespore is complete. Remains present throughout the late stages of morphogenesis and during this accumulation process preferentially collects on the mother cell side of the engulfed forespore, but eventually is deposited equally all around the forespore.3 Publications

    <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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Polymerizes to self-assemble into static filaments. ATP hydrolysis is required by every subunit for incorporation into the growing polymer by inducing a conformational change that drives polymerization of a nucleotide-free filament. Polymerization requires a critical concentration of the protein and only occurs after it is localized to the surface of the developing spore.

    Interacts (via extreme C-terminus Gly-486) with SpoVM (via Ile-6).

    Interacts (via full-length) with SpoVID (via C-terminus 499-575 AA).

    Interacts with SafA.

    5 Publications

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    224308.BSU22800

    <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

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi24 – 31Walker A motif; involved in ATP-binding and hydrolysis8

    <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

    Extreme C-terminal region (AA 487-492) is required for its proper localization into a spherical shell around the developing forespore. N-teminus (AA 1-64) is functionally important although largely dispensable for proper localization.1 Publication

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4105DXU Bacteria
    ENOG410XQ51 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000058353

    KEGG Orthology (KO)

    More...
    KOi
    K06398

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    RMVTTPW

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P35149

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR027417 P-loop_NTPase
    IPR014201 Spore_IV_A

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF09547 Spore_IV_A, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF007466 SpoIVA, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF52540 SSF52540, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR02836 spore_IV_A, 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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

    P35149-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MEKVDIFKDI AERTGGDIYL GVVGAVRTGK STFIKKFMEL VVLPNISNEA
    60 70 80 90 100
    DRARAQDELP QSAAGKTIMT TEPKFVPNQA MSVHVSDGLD VNIRLVDCVG
    110 120 130 140 150
    YTVPGAKGYE DENGPRMINT PWYEEPIPFH EAAEIGTRKV IQEHSTIGVV
    160 170 180 190 200
    ITTDGTIGDI ARSDYIEAEE RVIEELKEVG KPFIMVINSV RPYHPETEAM
    210 220 230 240 250
    RQDLSEKYDI PVLAMSVESM RESDVLSVLR EALYEFPVLE VNVNLPSWVM
    260 270 280 290 300
    VLKENHWLRE SYQESVKETV KDIKRLRDVD RVVGQFSEFE FIESAGLAGI
    310 320 330 340 350
    ELGQGVAEID LYAPDHLYDQ ILKEVVGVEI RGRDHLLELM QDFAHAKTEY
    360 370 380 390 400
    DQVSDALKMV KQTGYGIAAP ALADMSLDEP EIIRQGSRFG VRLKAVAPSI
    410 420 430 440 450
    HMIKVDVESE FAPIIGTEKQ SEELVRYLMQ DFEDDPLSIW NSDIFGRSLS
    460 470 480 490
    SIVREGIQAK LSLMPENARY KLKETLERII NEGSGGLIAI IL
    Length:492
    Mass (Da):55,175
    Last modified:February 1, 1994 - 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:i29EBA349DD18D12A
    GO

    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
    M81169 Genomic DNA Translation: AAA22802.1
    M80926 Genomic DNA Translation: AAB59029.1
    AL009126 Genomic DNA Translation: CAB14196.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A41970

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_390161.1, NC_000964.3
    WP_003230572.1, NZ_JNCM01000036.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    CAB14196; CAB14196; BSU22800

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    938991

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    bsu:BSU22800

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|224308.179.peg.2485

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <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
    M81169 Genomic DNA Translation: AAA22802.1
    M80926 Genomic DNA Translation: AAB59029.1
    AL009126 Genomic DNA Translation: CAB14196.1
    PIRiA41970
    RefSeqiNP_390161.1, NC_000964.3
    WP_003230572.1, NZ_JNCM01000036.1

    3D structure databases

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    SWISS-MODEL Interactive Workspace

    More...
    SWISS-MODEL-Workspacei
    Submit a new modelling project...

    Protein-protein interaction databases

    STRINGi224308.BSU22800

    Proteomic databases

    PaxDbiP35149
    PRIDEiP35149

    Genome annotation databases

    EnsemblBacteriaiCAB14196; CAB14196; BSU22800
    GeneIDi938991
    KEGGibsu:BSU22800
    PATRICifig|224308.179.peg.2485

    Phylogenomic databases

    eggNOGiENOG4105DXU Bacteria
    ENOG410XQ51 LUCA
    HOGENOMiHOG000058353
    KOiK06398
    OMAiRMVTTPW
    PhylomeDBiP35149

    Enzyme and pathway databases

    BioCyciBSUB:BSU22800-MONOMER

    Family and domain databases

    InterProiView protein in InterPro
    IPR027417 P-loop_NTPase
    IPR014201 Spore_IV_A
    PfamiView protein in Pfam
    PF09547 Spore_IV_A, 1 hit
    PIRSFiPIRSF007466 SpoIVA, 1 hit
    SUPFAMiSSF52540 SSF52540, 1 hit
    TIGRFAMsiTIGR02836 spore_IV_A, 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 nameiSP4A_BACSU
    <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: P35149
    <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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: February 1, 1994
    Last modified: December 11, 2019
    This is version 111 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
    UniProt is an ELIXIR core data resource
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