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Database: UniProt
Entry: K0N6C8_DESTT
LinkDB: K0N6C8_DESTT
Original site: K0N6C8_DESTT 
ID   K0N6C8_DESTT            Unreviewed;       475 AA.
AC   K0N6C8;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   22-NOV-2017, entry version 29.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   Name=apeA {ECO:0000313|EMBL:CCK79539.1};
GN   OrderedLocusNames=TOL2_C13760 {ECO:0000313|EMBL:CCK79539.1};
OS   Desulfobacula toluolica (strain DSM 7467 / Tol2).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC   Desulfobacteraceae; Desulfobacula.
OX   NCBI_TaxID=651182 {ECO:0000313|EMBL:CCK79539.1, ECO:0000313|Proteomes:UP000007347};
RN   [1] {ECO:0000313|EMBL:CCK79539.1, ECO:0000313|Proteomes:UP000007347}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7467 / Tol2 {ECO:0000313|Proteomes:UP000007347};
RX   PubMed=23088741; DOI=10.1111/j.1462-2920.2012.02885.x;
RA   Wohlbrand L., Jacob J.H., Kube M., Mussmann M., Jarling R., Beck A.,
RA   Amann R., Wilkes H., Reinhardt R., Rabus R.;
RT   "Complete genome, catabolic sub-proteomes and key-metabolites of
RT   Desulfobacula toluolica To12 marine, aromatic compound-degrading,
RT   sulfate-reducing bacterium.";
RL   Environ. Microbiol. 15:1334-1355(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; FO203503; CCK79539.1; -; Genomic_DNA.
DR   RefSeq; WP_014956886.1; NC_018645.1.
DR   MEROPS; M18.004; -.
DR   EnsemblBacteria; CCK79539; CCK79539; TOL2_C13760.
DR   KEGG; dto:TOL2_C13760; -.
DR   PATRIC; fig|651182.5.peg.1652; -.
DR   OMA; CFDHEEI; -.
DR   OrthoDB; POG091H01QL; -.
DR   Proteomes; UP000007347; 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:CCK79539.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007347};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:CCK79539.1};
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:UP000007347};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   475 AA;  52276 MW;  4A02ADBFC1A2C947 CRC64;
     MNKAQLKKIK DTILKKSPLV FDQLNKKQKS DLFKFNETYK QFLNKSKTER EAARQIITAA
     KARGFVDIDT LLENKTSSAK KVYKVFQGRC VALAVLGKEP LVFGANIIAS HIDSPRLDLK
     QNPIYEDLSM GLMKTHYYGG IRKYHWLAIP LALHGTIIKA DGETIDITIG EDPDDPVFTV
     TDLLPHLAGK IQANKKLSDA FEGEKLNLIA GSIPLGSDEE KNRFKLGVLN LLHETYKITE
     EDFVSAEIEA VPAGKARDVG FDKSMIGSYG QDDRICSYTS LEALLDQQSS DKTAIAMFFD
     KEEIGSEGNS GAKSSFLEDF MSDLLFISNQ NTDNRSLRKA LINSSCLSAD VNAAMDPDFK
     EVHEKLNAAK LGFGICMTKF TGVAGKSGSS DAGAEFVGKI RQIFNKNNIV WQTGELGKID
     QGGGGTVAKF LAKYGMNVLD CGPAILSMHS PFEVASKADV YMTYLGYKAF YAENR
//
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