(data stored in ACNUC7421 zone)

SWISSPROT: MAP1_ECO57

ID   MAP1_ECO57              Reviewed;         264 AA.
AC   P0AE20; P07906;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   05-JUL-2017, entry version 86.
DE   RecName: Full=Methionine aminopeptidase {ECO:0000255|HAMAP-Rule:MF_01974};
DE            Short=MAP {ECO:0000255|HAMAP-Rule:MF_01974};
DE            Short=MetAP {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};
GN   OrderedLocusNames=Z0178, ECs0170;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Removes the N-terminal methionine from nascent proteins.
CC       The N-terminal methionine is often cleaved when the second residue
CC       in the primary sequence is small and uncharged (Met-Ala-, Cys,
CC       Gly, Pro, Ser, Thr, or Val). Requires deformylation of the
CC       N(alpha)-formylated initiator methionine before it can be
CC       hydrolyzed. {ECO:0000255|HAMAP-Rule:MF_01974}.
CC   -!- CATALYTIC ACTIVITY: Release of N-terminal amino acids,
CC       preferentially methionine, from peptides and arylamides.
CC       {ECO:0000255|HAMAP-Rule:MF_01974}.
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-
CC       affinity and a low affinity metal-binding site. The true nature of
CC       the physiological cofactor is under debate. The enzyme is active
CC       with cobalt, zinc, manganese or divalent iron ions. Most likely,
CC       methionine aminopeptidases function as mononuclear Fe(2+)-
CC       metalloproteases under physiological conditions, and the
CC       catalytically relevant metal-binding site has been assigned to the
CC       histidine-containing high-affinity site. {ECO:0000255|HAMAP-
CC       Rule:MF_01974};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01974}.
CC   -!- SIMILARITY: Belongs to the peptidase M24A family. Methionine
CC       aminopeptidase type 1 subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_01974}.
DR   EMBL; AE005174; AAG54470.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33593.1; -; Genomic_DNA.
DR   PIR; B85501; B85501.
DR   PIR; B90650; B90650.
DR   RefSeq; NP_308197.1; NC_002695.1.
DR   RefSeq; WP_001018194.1; NZ_MWVM01000012.1.
DR   ProteinModelPortal; P0AE20; -.
DR   SMR; P0AE20; -.
DR   MINT; MINT-1219550; -.
DR   STRING; 155864.Z0178; -.
DR   EnsemblBacteria; AAG54470; AAG54470; Z0178.
DR   EnsemblBacteria; BAB33593; BAB33593; BAB33593.
DR   GeneID; 913847; -.
DR   KEGG; ece:Z0178; -.
DR   KEGG; ecs:ECs0170; -.
DR   PATRIC; fig|386585.9.peg.271; -.
DR   eggNOG; ENOG4105CA1; Bacteria.
DR   eggNOG; COG0024; LUCA.
DR   HOGENOM; HOG000030427; -.
DR   KO; K01265; -.
DR   SABIO-RK; P0AE20; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR   CDD; cd01086; MetAP1; 1.
DR   HAMAP; MF_01974; MetAP_1; 1.
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   3: Inferred from homology;
DR   PRODOM; P0AE20.
DR   SWISS-2DPAGE; P0AE20.
KW   Aminopeptidase; Complete proteome; Hydrolase; Metal-binding; Protease.
FT   CHAIN         1    264       Methionine aminopeptidase.
FT                                /FTId=PRO_0000148938.
FT   METAL        97     97       Divalent metal cation 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01974}.
FT   METAL       108    108       Divalent metal cation 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01974}.
FT   METAL       108    108       Divalent metal cation 2; catalytic.
FT                                {ECO:0000255|HAMAP-Rule:MF_01974}.
FT   METAL       171    171       Divalent metal cation 2; catalytic; via
FT                                tele nitrogen. {ECO:0000255|HAMAP-
FT                                Rule:MF_01974}.
FT   METAL       204    204       Divalent metal cation 2; catalytic.
FT                                {ECO:0000255|HAMAP-Rule:MF_01974}.
FT   METAL       235    235       Divalent metal cation 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01974}.
FT   METAL       235    235       Divalent metal cation 2; catalytic.
FT                                {ECO:0000255|HAMAP-Rule:MF_01974}.
FT   BINDING      79     79       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01974}.
FT   BINDING     178    178       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01974}.
SQ   SEQUENCE   264 AA;  29331 MW;  F2D0B57715A67851 CRC64;
     MAISIKTPED IEKMRVAGRL AAEVLEMIEP YVKPGVSTGE LDRICNDYIV NEQHAVSACL
     GYHGYPKSVC ISINEVVCHG IPDDAKLLKD GDIVNIDVTV IKDGFHGDTS KMFIVGKPTI
     MGERLCRITQ ESLYLALRMV KPGINLREIG AAIQKFVEAE GFSVVREYCG HGIGRGFHEE
     PQVLHYDSRE TNVVLKPGMT FTIEPMVNAG KKEIRTMKDG WTVKTKDRSL SAQYEHTIVV
     TDNGCEILTL RKDDTIPAII SHDE
//

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