ID   APEB_PSEPG              Reviewed;         429 AA.
AC   B0KTU0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=PputGB1_1322;
OS   Pseudomonas putida (strain GB-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=76869;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.;
RT   "Complete sequence of Pseudomonas putida GB-1.";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000255|HAMAP-
CC       Rule:MF_00467}.
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DR   EMBL; CP000926; ABY97229.1; -; Genomic_DNA.
DR   RefSeq; WP_012271003.1; NC_010322.1.
DR   AlphaFoldDB; B0KTU0; -.
DR   SMR; B0KTU0; -.
DR   STRING; 76869.PputGB1_1322; -.
DR   PRIDE; B0KTU0; -.
DR   EnsemblBacteria; ABY97229; ABY97229; PputGB1_1322.
DR   KEGG; ppg:PputGB1_1322; -.
DR   eggNOG; COG1362; Bacteria.
DR   HOGENOM; CLU_019532_2_0_6; -.
DR   OMA; GPILKVN; -.
DR   Proteomes; UP000002157; 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   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.30.250.10; -; 1.
DR   HAMAP; MF_00467; Aminopeptidase_M18_2; 1.
DR   InterPro; IPR022984; M18_aminopeptidase_2.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023358; Peptidase_M18_dom2.
DR   PANTHER; PTHR28570; PTHR28570; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
PE   3: Inferred from homology;
KW   Aminopeptidase; Hydrolase; Metal-binding; Metalloprotease; Protease; Zinc.
FT   CHAIN           1..429
FT                   /note="Probable M18 family aminopeptidase 2"
FT                   /id="PRO_1000081180"
FT   BINDING         82
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00467"
FT   BINDING         156
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00467"
FT   BINDING         401
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00467"
SQ   SEQUENCE   429 AA;  46883 MW;  D408FA5E58B05006 CRC64;
     MRDALNTGLI DFLKASPTPF HATASLAQRL EAAGYQRLDE RDSWATVPGG RYYVTRNDSS
     IIAIKLGKQA PLLNGIRMVG AHTDSPCLRV KPQPELQRQG FLQLGVEVYG GALLAPWFDR
     DLSLAGRVTY RRDGKVESQL IDFKLPIAII PNLAIHLNRT ANEGWAINPQ NELPPILAQV
     AGDERIDFRA LLTEQLAREH ELIADVVLDY ELSFYDTQDA ALIGLHGDFI AGARLDNLLS
     CYAGLQALLA ADSDETCVLV CNDHEEVGSC SACGADGPML EQTLQRLLPD GDSYVRTVQR
     SLMVSADNAH GVHPNYADKH DGNHGPKLNA GPVIKVNNNQ RYATNSETAG FFRHLCMAEE
     VPVQSFVVRS DMGCGSTIGP ITASHLGVRT VDIGLPTFAM HSIRELCGSH DLAHLVKVLT
     AFYRSRELP