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Database: UniProt
Entry: D1BM25_VEIPT
LinkDB: D1BM25_VEIPT
Original site: D1BM25_VEIPT 
ID   D1BM25_VEIPT            Unreviewed;       449 AA.
AC   D1BM25;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   07-JUN-2017, entry version 45.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   OrderedLocusNames=Vpar_0751 {ECO:0000313|EMBL:ACZ24432.1};
OS   Veillonella parvula (strain ATCC 10790 / DSM 2008 / JCM 12972 / Te3)
OS   (Veillonella alcalescens).
OC   Bacteria; Firmicutes; Negativicutes; Veillonellales; Veillonellaceae;
OC   Veillonella.
OX   NCBI_TaxID=479436 {ECO:0000313|EMBL:ACZ24432.1, ECO:0000313|Proteomes:UP000007968};
RN   [1] {ECO:0000313|Proteomes:UP000007968}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10790 / DSM 2008 / JCM 12972 / Te3
RC   {ECO:0000313|Proteomes:UP000007968};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA   Ivanova N., Mikhailova N., Saunders E., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.F.,
RA   Hugenholtz P., Woyke T., Wu D., Wellnitz S., Schneider S., Gronow S.,
RA   Klenk H.P., Eisen J.A.;
RT   "The complete genome of Veillonella parvula DSM 2008.";
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU004387};
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; CP001820; ACZ24432.1; -; Genomic_DNA.
DR   RefSeq; WP_012864230.1; NC_013520.1.
DR   ProteinModelPortal; D1BM25; -.
DR   STRING; 479436.Vpar_0751; -.
DR   MEROPS; M18.002; -.
DR   EnsemblBacteria; ACZ24432; ACZ24432; Vpar_0751.
DR   GeneID; 8636212; -.
DR   KEGG; vpr:Vpar_0751; -.
DR   PATRIC; fig|479436.6.peg.730; -.
DR   eggNOG; ENOG4105DFM; Bacteria.
DR   eggNOG; COG1362; LUCA.
DR   HOGENOM; HOG000253244; -.
DR   KO; K01267; -.
DR   OMA; CFDHEEI; -.
DR   BioCyc; VPAR479436:GHOS-765-MONOMER; -.
DR   Proteomes; UP000007968; Chromosome.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR001948; Peptidase_M18.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:ACZ24432.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007968};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|RuleBase:RU004386};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007968};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   449 AA;  49459 MW;  BC9A11E69FB63820 CRC64;
     MKFDNEQLLK YIGACTSPYH TVDTSLQMLL DSGFTELSLE DEWQLDSGSY VVNVFGTTLF
     AFHIGKKPEH TLRIASAHTD FPAIRVKPNP ITSMKGYTKL NVEMYGGLIE NTWLDRPLGA
     AGTVVLKGKN AFDVDSVLVD TKRPIAIVPN LAIHMNRSVN DGVKLNRQKE MLPILMMERN
     NEDNPTKPLN NRNNPSLFPE SDTQYDEWTK FLADEVDCDP SEILSYEMTL YPTEQGCVLG
     TEGDFISSPR LDNLTSCFSV LSGIIQAKKM NVNGVRCAIL FDNEEVGSRT KQGGAGMILP
     NLVKRVYDAL GYSNQEMDSF ISKGFMISSD VAHGLHPNYP EKNDITNIPV LNKGLSLKIA
     CSQSYAGDAK AIAIVKGLCE EADAQYQIYV NRSDIPGGST VGSISSAMLP MRTIDVGLPL
     LAMHSARELM GAADQEQLNR LMNHFLGGK
//
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