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Database: UniProt
Entry: G2FL77_9FIRM
LinkDB: G2FL77_9FIRM
Original site: G2FL77_9FIRM 
ID   G2FL77_9FIRM            Unreviewed;       437 AA.
AC   G2FL77;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   22-NOV-2017, entry version 28.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   Name=apeB {ECO:0000313|EMBL:EGW41585.1};
GN   ORFNames=DOT_0438 {ECO:0000313|EMBL:EGW41585.1};
OS   Desulfosporosinus sp. OT.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfosporosinus.
OX   NCBI_TaxID=913865 {ECO:0000313|EMBL:EGW41585.1, ECO:0000313|Proteomes:UP000004928};
RN   [1] {ECO:0000313|EMBL:EGW41585.1, ECO:0000313|Proteomes:UP000004928}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OT {ECO:0000313|EMBL:EGW41585.1,
RC   ECO:0000313|Proteomes:UP000004928};
RX   PubMed=21994931; DOI=10.1128/JB.06018-11;
RA   Abicht H.K., Mancini S., Karnachuk O.V., Solioz M.;
RT   "Genome Sequence of Desulfosporosinus sp. OT, an Acidophilic Sulfate-
RT   Reducing Bacterium from Copper Mining Waste in Norilsk, Northern
RT   Siberia.";
RL   J. Bacteriol. 193:6104-6105(2011).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EGW41585.1}.
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DR   EMBL; AGAF01000023; EGW41585.1; -; Genomic_DNA.
DR   RefSeq; WP_009613419.1; NZ_AGAF01000023.1.
DR   MEROPS; M18.002; -.
DR   EnsemblBacteria; EGW41585; EGW41585; DOT_0438.
DR   PATRIC; fig|913865.3.peg.398; -.
DR   OrthoDB; POG091H01I4; -.
DR   Proteomes; UP000004928; Unassembled WGS sequence.
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:EGW41585.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000004928};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:EGW41585.1};
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:UP000004928};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   437 AA;  48569 MW;  928C7BD4B58013F6 CRC64;
     MISYINNDEQ QFAQLLLNFI QESPSSFHVV EGIKKLLVPQ GFQTLSLKDK WSLIPGGKYY
     VTHNDSALIA FVVGEGVPEK YGFHIIGAHT DSPGFRVKPL PEISVEGHYV KLNVETYGEP
     ILNTWLDRPL SLAGRVILHG ESPFSPRIRL FRSDLPLLVI PNLAIHMNRK VNEGIELNKQ
     KDMLPLLSQI TQDFEKEGTL ISHLAKTLQC PTDDILDFDL FLYEYEKGRF FGLQQEFISS
     GRLDDLAMIH AGAWALANAK PTLTTQVLAC FDHEECGSTS KQGAASPFLS FILERILLGL
     KKDREEYLQA LAHSFLISAD MAHALHPNSG ERLDPVNRPI LNRGPVIKIS ANQNYTTDAE
     SAAVFTTLCQ LAGVPVQKFV NRSDERGGST IGPISTTHLD IRSVDIGNPV LAMHSVRELG
     GVKDHLAIAK VFSEFYK
//
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