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Database: UniProt
Entry: F2RCW0_STRVP
LinkDB: F2RCW0_STRVP
Original site: F2RCW0_STRVP 
ID   F2RCW0_STRVP            Unreviewed;       435 AA.
AC   F2RCW0;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-SEP-2017, entry version 39.
DE   RecName: Full=Probable M18 family aminopeptidase 2 {ECO:0000256|HAMAP-Rule:MF_00467};
DE            EC=3.4.11.- {ECO:0000256|HAMAP-Rule:MF_00467};
GN   Name=apeB {ECO:0000256|HAMAP-Rule:MF_00467};
GN   OrderedLocusNames=SVEN_3570 {ECO:0000313|EMBL:CCA56856.1};
OS   Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 /
OS   JCM 4526 / NBRC 13096 / PD 04745).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=953739 {ECO:0000313|EMBL:CCA56856.1, ECO:0000313|Proteomes:UP000006854};
RN   [1] {ECO:0000313|EMBL:CCA56856.1, ECO:0000313|Proteomes:UP000006854}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 /
RC   PD 04745 {ECO:0000313|Proteomes:UP000006854};
RX   PubMed=21463507; DOI=10.1186/1471-2164-12-175;
RA   Pullan S.T., Bibb M.J., Merrick M.;
RT   "Genome-wide analysis of the role of GlnR in Streptomyces venezuelae
RT   provides new insights into global nitrogen regulation in
RT   actinomycetes.";
RL   BMC Genomics 12:175-175(2011).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00467, ECO:0000256|RuleBase:RU004387};
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|HAMAP-Rule:MF_00467, ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; FR845719; CCA56856.1; -; Genomic_DNA.
DR   RefSeq; WP_015034771.1; NC_018750.1.
DR   MEROPS; M18.002; -.
DR   EnsemblBacteria; CCA56856; CCA56856; SVEN_3570.
DR   GeneID; 28671473; -.
DR   KEGG; sve:SVEN_3570; -.
DR   PATRIC; fig|953739.5.peg.5789; -.
DR   KO; K01267; -.
DR   OMA; CFDHEEI; -.
DR   OrthoDB; POG091H01I4; -.
DR   Proteomes; UP000006854; Chromosome.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00467; Aminopeptidase_M18_2; 1.
DR   InterPro; IPR022984; M18_aminopeptidase_2.
DR   InterPro; IPR001948; Peptidase_M18.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386, ECO:0000313|EMBL:CCA56856.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006854};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006854};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00467, ECO:0000256|RuleBase:RU004386}.
FT   METAL        92     92       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       163    163       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       411    411       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
SQ   SEQUENCE   435 AA;  46513 MW;  8B869FD6EB8AD064 CRC64;
     MTSAASRPTA GPFDRGHTDD LMAFLTASPS PYHAVASAAQ RLEKAGFRRV EETAAWDATT
     GGKYVIRGGA IIAWYVPEGA AAHTPYRIVG AHTDSPNLRV KPQPDMGAHG WRQVAVEIYG
     GTLLNTWLDR DLGLAGRLTL RDGSHHLVNV DRPLLRVPQL AIHLDRSAND GLKLERQRHM
     QPVWGTGEVH EGDLIEFVAA EAGVDAEDVS GWDLMVHAVE APAYLGRDRE LLAGPRMDNL
     LSVHAAVAAL ASLAGRDDLP YIPVLAAFDH EENGSEADTG AQGPLLGNVL ERSVYARGGS
     YEDRARAFAG TVCLSSDTGH AVHPNYAERH DPTHHPRVNG GPILKVNVNQ RYATDGSGRA
     VFAAACEKAG VPWQSFVSNN DMPCGTTIGP ITAARHGIRT VDIGVAILSM HSARELCGAE
     DPYLLANALV AFLEG
//
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