ID   APEB_PSEE4              Reviewed;         429 AA.
AC   Q1IDE6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 91.
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}; OrderedLocusNames=PSEEN1442;
OS   Pseudomonas entomophila (strain L48).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=384676;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L48;
RX   PubMed=16699499; DOI=10.1038/nbt1212;
RA   Vodovar N., Vallenet D., Cruveiller S., Rouy Z., Barbe V., Acosta C.,
RA   Cattolico L., Jubin C., Lajus A., Segurens B., Vacherie B., Wincker P.,
RA   Weissenbach J., Lemaitre B., Medigue C., Boccard F.;
RT   "Complete genome sequence of the entomopathogenic and metabolically
RT   versatile soil bacterium Pseudomonas entomophila.";
RL   Nat. Biotechnol. 24:673-679(2006).
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; CT573326; CAK14313.1; -; Genomic_DNA.
DR   RefSeq; WP_011532729.1; NC_008027.1.
DR   AlphaFoldDB; Q1IDE6; -.
DR   SMR; Q1IDE6; -.
DR   STRING; 384676.PSEEN1442; -.
DR   EnsemblBacteria; CAK14313; CAK14313; PSEEN1442.
DR   KEGG; pen:PSEEN1442; -.
DR   eggNOG; COG1362; Bacteria.
DR   HOGENOM; CLU_019532_2_0_6; -.
DR   OMA; GPILKVN; -.
DR   OrthoDB; 304020at2; -.
DR   Proteomes; UP000000658; 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_1000013703"
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;  46872 MW;  BDB3B7B15F24F1D4 CRC64;
     MRDALNAGLI EFLKASPTPF HATASLVQRL EAAGYQRLDE RDSWATVPGG RYYVTRNDSS
     IIAIKLGKLS PLLGGIRMVG AHTDSPCLRV KPQPELQRQG FLQLGVEVYG GALLAPWFDR
     DLSLAGRVTF RRDGKVESQL IDFKLPIAVI PNLAIHLNRT ANEGWQINPQ TELPPILAQV
     AGDERVDFRA LLTEQLAREH DLNADVVLDY ELSFYDTQDA ALIGLNGDFI AAARLDNLLS
     CYAGLQALLN ADSDETCVLV CNDHEEVGSC SACGADGPML EQTLQRLLPD GDDYVRAIQR
     SLMVSADNAH GVHPNYADKH DGNHGPKLNA GPVIKVNNNQ RYATNSETAG FFRHLCMAEE
     VPVQSFVVRS DMGCGSTIGP ITASHLGVRT VDIGLPTFAM HSIRELCGSH DLAHLVKVLT
     AFYRSRELP