ID   APEB_PSEMY              Reviewed;         429 AA.
AC   A4XRN0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=Pmen_1231;
OS   Pseudomonas mendocina (strain ymp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=399739;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ymp;
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., Kiss H., Brettin T., Detter J.C., Bruce D., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Hersman L., Dubois J., Maurice P., Richardson P.;
RT   "Complete sequence of Pseudomonas mendocina ymp.";
RL   Submitted (APR-2007) 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; CP000680; ABP83996.1; -; Genomic_DNA.
DR   RefSeq; WP_003241585.1; NC_009439.1.
DR   AlphaFoldDB; A4XRN0; -.
DR   SMR; A4XRN0; -.
DR   STRING; 399739.Pmen_1231; -.
DR   EnsemblBacteria; ABP83996; ABP83996; Pmen_1231.
DR   KEGG; pmy:Pmen_1231; -.
DR   PATRIC; fig|399739.8.peg.1243; -.
DR   eggNOG; COG1362; Bacteria.
DR   HOGENOM; CLU_019532_2_0_6; -.
DR   OMA; GPILKVN; -.
DR   OrthoDB; 304020at2; -.
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_1000013704"
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;  47014 MW;  8E5742D2BA9EE73D CRC64;
     MREELIQGLL DFLNASPTPF HATTSLAMRL EAAGYRHLDE RAPWHTEAGG RYYVTRNDSS
     IIAFKLGKRP VVEGGIRLVG AHTDSPCLRV KPSPELQRQG YFQLGVEVYG GALLAPWFDR
     DLSLAGRVTY RRDGKVESQL IDFYQPIAVI PNLAIHLNRE ANMGWAINAQ NELPPILAQL
     ASSETADFRA LLAEQLAMEH DFNPDAVLDY ELSFYDTQSA AIVGLNQDFI ASARLDNLLS
     CYAGLQALID SSDEETCVLV CTDHEEVGSC SACGADGPFL EQVLRRVLPE GDDFVRSIQR
     SLLVSADNAH GVHPNYADKH DGNHGPKLNA GPVIKINSNQ RYATNSETAG FFRHLCLENE
     VPVQSFVVRS DMACGSTIGP ITASQLGVRT VDIGLPTFAM HSIRELAGSH DVDHLVKVLT
     AFYSSPELP