GenomeNet

Database: UniProt
Entry: A5N8F0_CLOK5
LinkDB: A5N8F0_CLOK5
Original site: A5N8F0_CLOK5 
ID   A5N8F0_CLOK5            Unreviewed;       466 AA.
AC   A5N8F0;
DT   10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   10-JUL-2007, sequence version 1.
DT   07-JUN-2017, entry version 66.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   OrderedLocusNames=CKL_1539 {ECO:0000313|EMBL:EDK33581.1};
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:EDK33581.1, ECO:0000313|Proteomes:UP000002411};
RN   [1] {ECO:0000313|EMBL:EDK33581.1, 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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000673; EDK33581.1; -; Genomic_DNA.
DR   RefSeq; WP_012101931.1; NC_009706.1.
DR   ProteinModelPortal; A5N8F0; -.
DR   STRING; 431943.CKL_1539; -.
DR   MEROPS; M18.004; -.
DR   EnsemblBacteria; EDK33581; EDK33581; CKL_1539.
DR   KEGG; ckl:CKL_1539; -.
DR   eggNOG; ENOG4105DFM; Bacteria.
DR   eggNOG; COG1362; LUCA.
DR   HOGENOM; HOG000056589; -.
DR   OMA; YQWVTIP; -.
DR   OrthoDB; POG091H01QL; -.
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   Complete proteome {ECO:0000313|Proteomes:UP000002411};
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:UP000002411};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   466 AA;  52468 MW;  005DAF59130B2CCE CRC64;
     MSKDLTKKYK YAWDKYSKKD FKLLFELSDG YKDFMSRCKT ERECIREFIL RAEKNGYKDL
     ESIINEKAVL KPGDKVYANN KDKTLALFII GNKDIQEGMR ILGAHVDSPR IDLKQNPLYE
     DMDLALLDTH YYGGIKKYQW VTIPLAIHGV VVKKDGSKVE IVVGEKEDEP VVGISDLLVH
     LSSIQMEKKA NKVIEGEDLN ILVGSIPIQD KEAKDRVKQN ILRLLNDKYK IEEEDFVSAE
     LEVVPAGPAR DFGLDRSMIM AYGQDDRICA YTSFVAMMNI NNPDKTCATL LVDKEEIGSV
     GATGMHSRFF ENTVAEIIAL CGDYNDLKLR RVLTNSKMLS SDVSAAFDPN YPSVMEKNNS
     AYFGKGIVFN KYTGSKGKSG CNDANPEYIA ELRNIMEKDD VYWQTSELGK VDQGGGGTIA
     YILARYNMQV IDCGIALQNM HAPWEVASKA DIYEAVKGYT AFLNRI
//
DBGET integrated database retrieval system