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Database: UniProt
Entry: A0A0B3BSK4_9PSED
LinkDB: A0A0B3BSK4_9PSED
Original site: A0A0B3BSK4_9PSED 
ID   A0A0B3BSK4_9PSED        Unreviewed;       429 AA.
AC   A0A0B3BSK4;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-SEP-2017, entry version 15.
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=PT85_05920 {ECO:0000313|EMBL:KHO65590.1};
OS   Pseudomonas flexibilis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=706570 {ECO:0000313|EMBL:KHO65590.1, ECO:0000313|Proteomes:UP000030980};
RN   [1] {ECO:0000313|EMBL:KHO65590.1, ECO:0000313|Proteomes:UP000030980}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 14085 {ECO:0000313|EMBL:KHO65590.1,
RC   ECO:0000313|Proteomes:UP000030980};
RA   Shin S.-K., Yi H.;
RT   "Genome sequence of Pseudomonas tuomuerensis JCM 14085.";
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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:KHO65590.1}.
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DR   EMBL; JTAK01000002; KHO65590.1; -; Genomic_DNA.
DR   RefSeq; WP_039606169.1; NZ_JTAK01000002.1.
DR   EnsemblBacteria; KHO65590; KHO65590; PT85_05920.
DR   Proteomes; UP000030980; Unassembled WGS sequence.
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   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386, ECO:0000313|EMBL:KHO65590.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000030980};
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:UP000030980};
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;  46619 MW;  061AA958E9357A7A CRC64;
     MRAELTQGLI DFLKASPTPF HATATLAQRL EAAGYQPLDE RQPWQCEPGG RYYVTRNDSS
     LIAFKAGTRS PLEGGLRLVG AHTDSPCLRV KPQPEMQRHG FLQLGVEVYG GALLAPWFDR
     DLSLAGRVTF RRDGRVESQL IDFQAPIAVI PNLAIHLNRE ANQGWAINAQ NELPPILAQI
     AGAEPYDFRA LLADQLSREH ELTADIILDF ELSLYDTQPA AVVGLHGDFI AGARLDNLLS
     CYAGLQALLA ADDEQSCVLV CTDHEEVGST SCCGADGPFL EQTLERAFAA GEDLVRITQR
     SLLISADNAH GLHPNYPDKH DGNHGPKLNA GPVIKVNSNQ RYATSSETAG FFRHLCLENE
     VPMQSFVTRS DMGCGSTIGP ITASRLGVPT VDIGLPTFAM HSIRELAGSQ DLEHLVKVLT
     AFYNSAELA
//
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