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Database: UniProt
Entry: APEB_PSEFS
LinkDB: APEB_PSEFS
Original site: APEB_PSEFS 
ID   APEB_PSEFS              Reviewed;         429 AA.
AC   C3K0D7;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   22-NOV-2017, entry version 55.
DE   RecName: Full=Probable M18 family aminopeptidase 2 {ECO:0000255|HAMAP-Rule:MF_00467};
DE            EC=3.4.11.- {ECO:0000255|HAMAP-Rule:MF_00467};
GN   Name=apeB {ECO:0000255|HAMAP-Rule:MF_00467};
GN   OrderedLocusNames=PFLU_4373;
OS   Pseudomonas fluorescens (strain SBW25).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=216595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SBW25;
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00467};
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00467}.
DR   EMBL; AM181176; CAY51001.1; -; Genomic_DNA.
DR   RefSeq; WP_015885134.1; NC_012660.1.
DR   ProteinModelPortal; C3K0D7; -.
DR   SMR; C3K0D7; -.
DR   STRING; 216595.PFLU4373; -.
DR   PRIDE; C3K0D7; -.
DR   EnsemblBacteria; CAY51001; CAY51001; PFLU_4373.
DR   KEGG; pfs:PFLU_4373; -.
DR   PATRIC; fig|216595.4.peg.4517; -.
DR   eggNOG; ENOG4105DFM; Bacteria.
DR   eggNOG; COG1362; LUCA.
DR   KO; K01267; -.
DR   OMA; CFDHEEI; -.
DR   OrthoDB; POG091H01I4; -.
DR   Proteomes; UP000002332; 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   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; Complete proteome; Hydrolase; Metal-binding;
KW   Metalloprotease; Protease; Zinc.
FT   CHAIN         1    429       Probable M18 family aminopeptidase 2.
FT                                /FTId=PRO_1000206331.
FT   METAL        82     82       Zinc. {ECO:0000255|HAMAP-Rule:MF_00467}.
FT   METAL       156    156       Zinc. {ECO:0000255|HAMAP-Rule:MF_00467}.
FT   METAL       401    401       Zinc. {ECO:0000255|HAMAP-Rule:MF_00467}.
SQ   SEQUENCE   429 AA;  46943 MW;  4F60DA483052892F CRC64;
     MREALNQGLI DFLKASPTPF HATAALAQRL EAAGYQRLDE RETWTTEPNG RYYVTRNDSS
     IIAFKLGRHS PLQGGIRLVG AHTDSPCLRV KPQPELQRQG FWQLGVEVYG GALLAPWFDR
     DLSLAGRVTF RRDGKVESQL IDFKLPIAII PNLAIHLNRE ANQGWAINAQ TELPPILAQF
     AGDERVDFRA VLTDQLAREH GLNADVVLDY ELSFYDTQSA AVIGLNGDFI AGARLDNLLS
     CYAGLQALLT SETDETCVLV CNDHEEVGSC SACGADGPML EQTLRRLLPE GDEFVRTIQK
     SLLVSADNAH GVHPNYAEKH DANHGPKLNA GPVIKVNSNQ RYATNSETAG FFRHLCMAQE
     VPVQSFVVRS DMGCGSTIGP ITASHLGVRT VDIGLPTFAM HSIRELCGSH DLAHLVKVLG
     AFYASHDLP
//
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