GenomeNet

Database: UniProt
Entry: A0A077LCN9_9PSED
LinkDB: A0A077LCN9_9PSED
Original site: A0A077LCN9_9PSED 
ID   A0A077LCN9_9PSED        Unreviewed;       429 AA.
AC   A0A077LCN9;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   25-OCT-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=PSCI_0131 {ECO:0000313|EMBL:BAP40833.1};
OS   Pseudomonas sp. StFLB209.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1028989 {ECO:0000313|EMBL:BAP40833.1, ECO:0000313|Proteomes:UP000031652};
RN   [1] {ECO:0000313|Proteomes:UP000031652}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=StFLB209 {ECO:0000313|Proteomes:UP000031652};
RA   Morohoshi T., Kato T., Someya N., Ikeda T.;
RT   "Complete Genome Sequence of N-Acylhomoserine Lactone-Producing
RT   Pseudomonas sp. Strain StFLB209, Isolated from Potato Phyllosphere.";
RL   Genome Announc.2:e01037-14(2014).
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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AP014637; BAP40833.1; -; Genomic_DNA.
DR   RefSeq; WP_045481454.1; NZ_AP014637.1.
DR   EnsemblBacteria; BAP40833; BAP40833; PSCI_0131.
DR   KEGG; pses:PSCI_0131; -.
DR   KO; K01267; -.
DR   Proteomes; UP000031652; 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   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:BAP40833.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000031652};
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:UP000031652};
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;  47015 MW;  93CB70D989E3889B CRC64;
     MREELNKGLI DFLKASPTPF HATATLVQHL EAGGFQRLDE RDTWAVEAGG RYYVTRNDSS
     VVAWRMGRHS PLISGIRMVG AHTDSPCLRV KPQPELQRQG FWQLGVEVYG GALLAPWFDR
     DLSLAGRVTF RRDGKVESQL VNFKQPIAVI PNLAIHLNRT ANEGWQINPQ IELPPILAQV
     AGDERPDFRA LLTDQLAREH DLNADVVLDY ELSFYDTQSA AVIGLNGDFI AGARLDNLLS
     CYAGLQALLG SDSEETCLLV CTDHEEIGSA SACGADGPML EQIVQRLVSD HEDYVRTIQR
     SLLISADNAH GVHPNYADKH DGNHGPKLNA GPVIKVNNNQ RYATNSETAG FFRHLCMAVE
     VPVQSFVVRS DMGCGSTIGP ITASHLGIRT VDIGLPTFAM HSIRELAGSH DLAHLVKVLG
     AFYTSNELP
//
DBGET integrated database retrieval system