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Database: UniProt
Entry: S6A870_9SPIO
LinkDB: S6A870_9SPIO
Original site: S6A870_9SPIO 
ID   S6A870_9SPIO            Unreviewed;       432 AA.
AC   S6A870;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   22-NOV-2017, entry version 26.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=TPE_0818 {ECO:0000313|EMBL:AGT43314.1};
OS   Treponema pedis str. T A4.
OC   Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema.
OX   NCBI_TaxID=1291379 {ECO:0000313|EMBL:AGT43314.1, ECO:0000313|Proteomes:UP000015620};
RN   [1] {ECO:0000313|EMBL:AGT43314.1, ECO:0000313|Proteomes:UP000015620}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T A4 {ECO:0000313|EMBL:AGT43314.1};
RX   PubMed=23977007; DOI=10.1371/journal.pone.0071281;
RA   Svartstrom O., Mushtaq M., Pringle M., Segerman B.;
RT   "Genome-Wide Relatedness of Treponema pedis, from Gingiva and Necrotic
RT   Skin Lesions of Pigs, with the Human Oral Pathogen Treponema
RT   denticola.";
RL   PLoS ONE 8:E71281-E71281(2013).
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; CP004120; AGT43314.1; -; Genomic_DNA.
DR   MEROPS; M18.002; -.
DR   EnsemblBacteria; AGT43314; AGT43314; TPE_0818.
DR   KEGG; tped:TPE_0818; -.
DR   PATRIC; fig|1291379.3.peg.814; -.
DR   KO; K01267; -.
DR   OrthoDB; POG091H01I4; -.
DR   BioCyc; TPED1291379:G13GX-823-MONOMER; -.
DR   Proteomes; UP000015620; 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   InterPro; IPR023367; Peptidase_M42_dom2.
DR   PANTHER; PTHR28570; PTHR28570; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SUPFAM; SSF101821; SSF101821; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:AGT43314.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000015620};
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:UP000015620};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   432 AA;  48037 MW;  8E3295FCC3993EE2 CRC64;
     MNKQYAEALM KFIDKSPSVY HAIKNLGEFL EANGFNRLEQ KDSFNLKEGG KYFITNNGSA
     VIAWQMPKTG GAENGFRIIG SHSDSPTFRI KPNPEIKVNN HFLKLNTEVY GGAILSTWFD
     RPLSAAGRAV LKTDNLLKPE IRLIDFDKPI LIIPNLAIHM NREVNEGYSY NKQKDTLPVL
     SIINEKFEEK GFLLNLIAEN LNVKKEQILD FDLYLYDRQP GCFVGLNDEF FSIGRIDNLG
     MAYSSIDALA RSRASTFVQM AAVFDNEEVG SGTAQGAGSP FLQDTIQRIV LSTCKGNAFE
     EMQKALAFSF LISADQAHGL HPNYTEKNDI TNFPLMNKGP AIKLAASMSY TSDGISAGIF
     KDVCMRAKVP FQNFVNRSDM RGGSTIGPIS VSNLNIKSVD IGNPILAMHS VRELGGTEDQ
     EFITKAFEEF YK
//
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