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Database: UniProt
Entry: A0A0K1XDC7_9GAMM
LinkDB: A0A0K1XDC7_9GAMM
Original site: A0A0K1XDC7_9GAMM 
ID   A0A0K1XDC7_9GAMM        Unreviewed;       429 AA.
AC   A0A0K1XDC7;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   22-NOV-2017, entry version 16.
DE   RecName: Full=Probable M18 family aminopeptidase 2 {ECO:0000256|HAMAP-Rule:MF_00467};
DE            EC=3.4.11.- {ECO:0000256|HAMAP-Rule:MF_00467};
GN   Name=apeB {ECO:0000256|HAMAP-Rule:MF_00467};
GN   ORFNames=AKN88_03900 {ECO:0000313|EMBL:AKX59178.1};
OS   Oblitimonas alkaliphila.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Oblitimonas.
OX   NCBI_TaxID=1697053 {ECO:0000313|EMBL:AKX59178.1, ECO:0000313|Proteomes:UP000063953};
RN   [1] {ECO:0000313|EMBL:AKX59178.1, ECO:0000313|Proteomes:UP000063953}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E5571 {ECO:0000313|EMBL:AKX59178.1,
RC   ECO:0000313|Proteomes:UP000063953};
RX   PubMed=26679585;
RA   Lauer A.C., Nicholson A.C., Humrighouse B.W., Emery B., Drobish A.,
RA   Juieng P., Loparev V., McQuiston J.R.;
RT   "Genome Sequences of Oblitimonas alkaliphila gen. nov. sp. nov.
RT   (Proposed), a Novel Bacterium of the Pseudomonadaceae Family.";
RL   Genome Announc. 3:e01474-15(2015).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00467, ECO:0000256|RuleBase:RU004387};
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|HAMAP-Rule:MF_00467, ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; CP012365; AKX59178.1; -; Genomic_DNA.
DR   RefSeq; WP_053100245.1; NZ_CP012365.1.
DR   EnsemblBacteria; AKX59178; AKX59178; AKN88_03900.
DR   KEGG; pbb:AKN87_05885; -.
DR   PATRIC; fig|1697052.3.peg.2116; -.
DR   KO; K01267; -.
DR   Proteomes; UP000063953; Chromosome.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00467; Aminopeptidase_M18_2; 1.
DR   InterPro; IPR022984; M18_aminopeptidase_2.
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|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386, ECO:0000313|EMBL:AKX59178.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000063953};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386};
KW   Reference proteome {ECO:0000313|Proteomes:UP000063953};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00467, ECO:0000256|RuleBase:RU004386}.
FT   METAL        82     82       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       156    156       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       401    401       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
SQ   SEQUENCE   429 AA;  46951 MW;  A3D00CC150144085 CRC64;
     MKLSLSQGLI DFLHLSPTPF HATETMASNL EAAGFQALDE KQPWDLVPGG QYYITRNNSS
     IIALKLGLNA LEDSGFRVVG AHTDSPCLKV KPNADLTQHG YWQLGVEVYG GALLSPWFDR
     DLSLAGRVTF SVHGKLHSKL INFQTPIAVI PSLAIHLNRE ANRGWELNPQ KELPPIVAQL
     NSGEQADLHA MLSLQIEREH GIEHADILDF ELYFYDTQPA AMIGFEEDFI AGARLDNLLS
     CYAGLHALLE SDDSQTSILV CTDHEEVGSS SACGADGPFL EQVIQRLLPN AEQRFIAIQQ
     SLLISADNAH GIHPNYPEKH DANHGPLLNH GPVIKINANQ RYATNSHTAG FFRLLCQQEM
     IPVQSFVTRS DMSCGSTIGP ITASKLGINT LDIGVPTFAM HSIRELAGTD DLAHLVKALT
     AFYNSESCE
//
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