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P19994

- MAP11_BACSU

UniProt

P19994 - MAP11_BACSU

Protein

Methionine aminopeptidase 1

Gene

map

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 1 (01 Feb 1991)
      Previous versions | rss
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    Functioni

    Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed.1 PublicationUniRule annotation

    Catalytic activityi

    Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.1 PublicationUniRule annotation

    Cofactori

    Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe2+-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site.UniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei77 – 771SubstrateUniRule annotation
    Metal bindingi94 – 941Divalent metal cation 1UniRule annotation
    Metal bindingi105 – 1051Divalent metal cation 1UniRule annotation
    Metal bindingi105 – 1051Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi168 – 1681Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei175 – 1751SubstrateUniRule annotation
    Metal bindingi201 – 2011Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi232 – 2321Divalent metal cation 1UniRule annotation
    Metal bindingi232 – 2321Divalent metal cation 2; catalyticUniRule annotation

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-HAMAP
    2. metalloaminopeptidase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. protein initiator methionine removal Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Protease

    Keywords - Ligandi

    Metal-binding

    Enzyme and pathway databases

    BioCyciBSUB:BSU01380-MONOMER.

    Protein family/group databases

    MEROPSiM24.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methionine aminopeptidase 1UniRule annotation (EC:3.4.11.18UniRule annotation)
    Short name:
    MAP 1UniRule annotation
    Short name:
    MetAP 1UniRule annotation
    Alternative name(s):
    Peptidase MUniRule annotation
    Gene namesi
    Name:mapUniRule annotation
    Ordered Locus Names:BSU01380
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU01380. [Micado]

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 248248Methionine aminopeptidase 1PRO_0000148927Add
    BLAST

    Proteomic databases

    PaxDbiP19994.

    Expressioni

    Inductioni

    Expression increases gradually during the log phase of growth.1 Publication

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi224308.BSU01380.

    Structurei

    3D structure databases

    ProteinModelPortaliP19994.
    SMRiP19994. Positions 1-247.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0024.
    HOGENOMiHOG000030426.
    KOiK01265.
    OMAiNIIQTHA.
    OrthoDBiEOG6MWNDS.
    PhylomeDBiP19994.

    Family and domain databases

    Gene3Di3.90.230.10. 1 hit.
    HAMAPiMF_01974. MetAP_1.
    InterProiIPR001714. Pept_M24_MAP.
    IPR000994. Pept_M24_structural-domain.
    IPR002467. Pept_M24A_MAP1.
    [Graphical view]
    PfamiPF00557. Peptidase_M24. 1 hit.
    [Graphical view]
    PRINTSiPR00599. MAPEPTIDASE.
    SUPFAMiSSF55920. SSF55920. 1 hit.
    TIGRFAMsiTIGR00500. met_pdase_I. 1 hit.
    PROSITEiPS00680. MAP_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P19994-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIICKTPREL GIMREAGRIV ALTHEELKKH IKPGISTKEL DQIAERFIKK    50
    QGAIPSFKGY NGFRGSICVS VNEELVHGIP GSRVLKDGDI ISIDIGAKLN 100
    GYHGDSAWTY PVGNISDDDK KLLEVTEESL YKGLQEAKPG ERLSNISHAI 150
    QTYVENEQFS VVREYVGHGV GQDLHEDPQI PHYGPPNKGP RLKPGMVLAI 200
    EPMVNAGSRY VKTLADNWTV VTVDGKKCAH FEHTIAITET GFDILTRV 248
    Length:248
    Mass (Da):27,409
    Last modified:February 1, 1991 - v1
    Checksum:i6D6F7A593D84A761
    GO

    Mass spectrometryi

    Molecular mass is 27409.17±0.92 Da from positions 1 - 248. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D00619 Genomic DNA. Translation: BAA00497.1.
    L47971 Genomic DNA. Translation: AAB06821.1.
    AL009126 Genomic DNA. Translation: CAB11914.1.
    PIRiJS0493.
    RefSeqiNP_388019.1. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB11914; CAB11914; BSU01380.
    GeneIDi938929.
    KEGGibsu:BSU01380.
    PATRICi18971785. VBIBacSub10457_0141.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D00619 Genomic DNA. Translation: BAA00497.1 .
    L47971 Genomic DNA. Translation: AAB06821.1 .
    AL009126 Genomic DNA. Translation: CAB11914.1 .
    PIRi JS0493.
    RefSeqi NP_388019.1. NC_000964.3.

    3D structure databases

    ProteinModelPortali P19994.
    SMRi P19994. Positions 1-247.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU01380.

    Protein family/group databases

    MEROPSi M24.001.

    Proteomic databases

    PaxDbi P19994.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB11914 ; CAB11914 ; BSU01380 .
    GeneIDi 938929.
    KEGGi bsu:BSU01380.
    PATRICi 18971785. VBIBacSub10457_0141.

    Organism-specific databases

    GenoListi BSU01380. [Micado ]

    Phylogenomic databases

    eggNOGi COG0024.
    HOGENOMi HOG000030426.
    KOi K01265.
    OMAi NIIQTHA.
    OrthoDBi EOG6MWNDS.
    PhylomeDBi P19994.

    Enzyme and pathway databases

    BioCyci BSUB:BSU01380-MONOMER.

    Family and domain databases

    Gene3Di 3.90.230.10. 1 hit.
    HAMAPi MF_01974. MetAP_1.
    InterProi IPR001714. Pept_M24_MAP.
    IPR000994. Pept_M24_structural-domain.
    IPR002467. Pept_M24A_MAP1.
    [Graphical view ]
    Pfami PF00557. Peptidase_M24. 1 hit.
    [Graphical view ]
    PRINTSi PR00599. MAPEPTIDASE.
    SUPFAMi SSF55920. SSF55920. 1 hit.
    TIGRFAMsi TIGR00500. met_pdase_I. 1 hit.
    PROSITEi PS00680. MAP_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of a Bacillus subtilis gene homologous to E. coli secY."
      Nakamura K., Nakamura A., Takamatsu H., Yoshikawa H., Yamane K.
      J. Biochem. 107:603-607(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Genetic and transcriptional organization of the Bacillus subtilis spc-alpha region."
      Suh J.-W., Boylan S.A., Oh S.H., Price C.W.
      Gene 169:17-23(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.
    3. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
      Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
      , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
      Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.
    4. "The two authentic methionine aminopeptidase genes are differentially expressed in Bacillus subtilis."
      You C., Lu H., Sekowska A., Fang G., Wang Y., Gilles A.-M., Danchin A.
      BMC Microbiol. 5:57-57(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, MASS SPECTROMETRY, COFACTOR, INDUCTION, SUBCELLULAR LOCATION.
      Strain: 168.

    Entry informationi

    Entry nameiMAP11_BACSU
    AccessioniPrimary (citable) accession number: P19994
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: February 1, 1991
    Last modified: October 1, 2014
    This is version 120 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3