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Database: UniProt
Entry: A5N4D1_CLOK5
LinkDB: A5N4D1_CLOK5
Original site: A5N4D1_CLOK5 
ID   A5N4D1_CLOK5            Unreviewed;       434 AA.
AC   A5N4D1;
DT   10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   10-JUL-2007, sequence version 1.
DT   07-JUN-2017, entry version 67.
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:EDK32162.1};
GN   OrderedLocusNames=CKL_0085 {ECO:0000313|EMBL:EDK32162.1};
OS   Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=431943 {ECO:0000313|EMBL:EDK32162.1, ECO:0000313|Proteomes:UP000002411};
RN   [1] {ECO:0000313|EMBL:EDK32162.1, ECO:0000313|Proteomes:UP000002411}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8527 / DSM 555 / NCIMB 10680
RC   {ECO:0000313|Proteomes:UP000002411};
RX   PubMed=18218779; DOI=10.1073/pnas.0711093105;
RA   Seedorf H., Fricke W.F., Veith B., Brueggemann H., Liesegang H.,
RA   Strittmatter A., Miethke M., Buckel W., Hinderberger J., Li F.,
RA   Hagemeier C., Thauer R.K., Gottschalk G.;
RT   "The genome of Clostridium kluyveri, a strict anaerobe with unique
RT   metabolic features.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:2128-2133(2008).
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; CP000673; EDK32162.1; -; Genomic_DNA.
DR   RefSeq; WP_011988688.1; NC_009706.1.
DR   ProteinModelPortal; A5N4D1; -.
DR   STRING; 431943.CKL_0085; -.
DR   MEROPS; M18.002; -.
DR   EnsemblBacteria; EDK32162; EDK32162; CKL_0085.
DR   KEGG; ckl:CKL_0085; -.
DR   eggNOG; ENOG4105DFM; Bacteria.
DR   eggNOG; COG1362; LUCA.
DR   HOGENOM; HOG000253244; -.
DR   KO; K01267; -.
DR   OMA; CFDHEEI; -.
DR   OrthoDB; POG091H01I4; -.
DR   Proteomes; UP000002411; 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:EDK32162.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002411};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:EDK32162.1};
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:UP000002411};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   434 AA;  48423 MW;  23A10C209722069C CRC64;
     MKNYEIEEAE ELIDYIYESP TAFHAVKNAV NLLKKSGFIE IKEENSWNLK KGGKYFITKN
     DSALIAFTVG NGEIEKDGFR IIGAHTDSPC FKIKPNADIN VENNYIKINT EVYGGPILNT
     WMDRPLAMAG RIVLKSKDPF YPHSSLINIA KPLMIIPNLA IHMNRDVNSG IKLSKQKHML
     PLLTLVNSNS KNKHCLIEII CEELSIAKEN ILDFDLFLYE FGKGTIMGAN REFISSGRLD
     DLSMVYSGIK SISDTKVKNS TNVMVCFDNE EVGSTTKQGA NSPMLLSLLE RIVFNLGKNK
     DQFYRAISKS FMISCDLGHA LHPNYIEKSD PANRPIVNKG PIIKISASQS YTTDGVSGAI
     YKSICDRANI PVQIFVNHSD ERGGSTIGPI SSSHINMTCV DMGIPILSMH SIRELAGVKD
     YVYAMNSFKT FYNF
//
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