(data stored in ACNUC7421 zone)

SWISSPROT: MAP11_BACSU

ID   MAP11_BACSU             Reviewed;         248 AA.
AC   P19994;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   11-DEC-2019, entry version 147.
DE   RecName: Full=Methionine aminopeptidase 1 {ECO:0000255|HAMAP-Rule:MF_01974};
DE            Short=MAP 1 {ECO:0000255|HAMAP-Rule:MF_01974};
DE            Short=MetAP 1 {ECO:0000255|HAMAP-Rule:MF_01974};
DE            EC=3.4.11.18 {ECO:0000255|HAMAP-Rule:MF_01974};
DE   AltName: Full=Peptidase M {ECO:0000255|HAMAP-Rule:MF_01974};
GN   Name=map {ECO:0000255|HAMAP-Rule:MF_01974}; OrderedLocusNames=BSU01380;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2113521; DOI=10.1093/oxfordjournals.jbchem.a123093;
RA   Nakamura K., Nakamura A., Takamatsu H., Yoshikawa H., Yamane K.;
RT   "Cloning and characterization of a Bacillus subtilis gene homologous to E.
RT   coli secY.";
RL   J. Biochem. 107:603-607(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC   3610 / VKM B-501;
RX   PubMed=8635744; DOI=10.1016/0378-1119(95)00757-1;
RA   Suh J.-W., Boylan S.A., Oh S.H., Price C.W.;
RT   "Genetic and transcriptional organization of the Bacillus subtilis spc-
RT   alpha region.";
RL   Gene 169:17-23(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, MASS SPECTROMETRY, COFACTOR, INDUCTION, AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=168;
RX   PubMed=16207374; DOI=10.1186/1471-2180-5-57;
RA   You C., Lu H., Sekowska A., Fang G., Wang Y., Gilles A.-M., Danchin A.;
RT   "The two authentic methionine aminopeptidase genes are differentially
RT   expressed in Bacillus subtilis.";
RL   BMC Microbiol. 5:57-57(2005).
CC   -!- FUNCTION: Removes the N-terminal methionine from nascent proteins. The
CC       N-terminal methionine is often cleaved when the second residue in the
CC       primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser,
CC       Thr, or Val). Requires deformylation of the N(alpha)-formylated
CC       initiator methionine before it can be hydrolyzed. {ECO:0000255|HAMAP-
CC       Rule:MF_01974, ECO:0000269|PubMed:16207374}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of N-terminal amino acids, preferentially methionine,
CC         from peptides and arylamides.; EC=3.4.11.18;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01974,
CC         ECO:0000269|PubMed:16207374};
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01974};
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01974};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01974};
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01974};
CC       Note=Binds 2 divalent metal cations per subunit. Has a high-affinity
CC       and a low affinity metal-binding site. The true nature of the
CC       physiological cofactor is under debate. The enzyme is active with
CC       cobalt, zinc, manganese or divalent iron ions. Most likely, methionine
CC       aminopeptidases function as mononuclear Fe(2+)-metalloproteases under
CC       physiological conditions, and the catalytically relevant metal-binding
CC       site has been assigned to the histidine-containing high-affinity site.
CC       {ECO:0000255|HAMAP-Rule:MF_01974};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01974}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16207374}.
CC   -!- INDUCTION: Expression increases gradually during the log phase of
CC       growth. {ECO:0000269|PubMed:16207374}.
CC   -!- MASS SPECTROMETRY: Mass=27409.17; Mass_error=0.92; Method=Unknown;
CC       Evidence={ECO:0000269|PubMed:16207374};
CC   -!- SIMILARITY: Belongs to the peptidase M24A family. Methionine
CC       aminopeptidase type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_01974}.
DR   EMBL; D00619; BAA00497.1; -; Genomic_DNA.
DR   EMBL; L47971; AAB06821.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11914.1; -; Genomic_DNA.
DR   PIR; JS0493; JS0493.
DR   RefSeq; NP_388019.1; NC_000964.3.
DR   RefSeq; WP_003225828.1; NZ_JNCM01000029.1.
DR   SMR; P19994; -.
DR   STRING; 224308.BSU01380; -.
DR   jPOST; P19994; -.
DR   PaxDb; P19994; -.
DR   PRIDE; P19994; -.
DR   EnsemblBacteria; CAB11914; CAB11914; BSU01380.
DR   GeneID; 938929; -.
DR   KEGG; bsu:BSU01380; -.
DR   PATRIC; fig|224308.179.peg.141; -.
DR   eggNOG; ENOG4105CA1; Bacteria.
DR   eggNOG; COG0024; LUCA.
DR   HOGENOM; HOG000030426; -.
DR   InParanoid; P19994; -.
DR   KO; K01265; -.
DR   OMA; SYFHGPP; -.
DR   PhylomeDB; P19994; -.
DR   BioCyc; BSUB:BSU01380-MONOMER; -.
DR   PRO; PR:P19994; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0070084; P:protein initiator methionine removal; IEA:UniProtKB-UniRule.
DR   CDD; cd01086; MetAP1; 1.
DR   Gene3D; 3.90.230.10; -; 1.
DR   HAMAP; MF_01974; MetAP_1; 1.
DR   InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR   InterPro; IPR000994; Pept_M24.
DR   InterPro; IPR001714; Pept_M24_MAP.
DR   InterPro; IPR002467; Pept_M24A_MAP1.
DR   Pfam; PF00557; Peptidase_M24; 1.
DR   PRINTS; PR00599; MAPEPTIDASE.
DR   SUPFAM; SSF55920; SSF55920; 1.
DR   TIGRFAMs; TIGR00500; met_pdase_I; 1.
DR   PROSITE; PS00680; MAP_1; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P19994.
DR   SWISS-2DPAGE; P19994.
KW   Aminopeptidase; Cytoplasm; Hydrolase; Metal-binding; Protease;
KW   Reference proteome.
FT   CHAIN           1..248
FT                   /note="Methionine aminopeptidase 1"
FT                   /id="PRO_0000148927"
FT   METAL           94
FT                   /note="Divalent metal cation 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01974"
FT   METAL           105
FT                   /note="Divalent metal cation 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01974"
FT   METAL           105
FT                   /note="Divalent metal cation 2; catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01974"
FT   METAL           168
FT                   /note="Divalent metal cation 2; catalytic; via tele
FT                   nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01974"
FT   METAL           201
FT                   /note="Divalent metal cation 2; catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01974"
FT   METAL           232
FT                   /note="Divalent metal cation 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01974"
FT   METAL           232
FT                   /note="Divalent metal cation 2; catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01974"
FT   BINDING         77
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01974"
FT   BINDING         175
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01974"
SQ   SEQUENCE   248 AA;  27409 MW;  6D6F7A593D84A761 CRC64;
     MIICKTPREL GIMREAGRIV ALTHEELKKH IKPGISTKEL DQIAERFIKK QGAIPSFKGY
     NGFRGSICVS VNEELVHGIP GSRVLKDGDI ISIDIGAKLN GYHGDSAWTY PVGNISDDDK
     KLLEVTEESL YKGLQEAKPG ERLSNISHAI QTYVENEQFS VVREYVGHGV GQDLHEDPQI
     PHYGPPNKGP RLKPGMVLAI EPMVNAGSRY VKTLADNWTV VTVDGKKCAH FEHTIAITET
     GFDILTRV
//

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