ID   APEB_PSEA7              Reviewed;         429 AA.
AC   A6V2H4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=PSPA7_1878;
OS   Pseudomonas aeruginosa (strain PA7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=381754;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PA7;
RA   Dodson R.J., Harkins D., Paulsen I.T.;
RL   Submitted (JUN-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; CP000744; ABR81680.1; -; Genomic_DNA.
DR   RefSeq; WP_003150358.1; NC_009656.1.
DR   AlphaFoldDB; A6V2H4; -.
DR   SMR; A6V2H4; -.
DR   PRIDE; A6V2H4; -.
DR   EnsemblBacteria; ABR81680; ABR81680; PSPA7_1878.
DR   KEGG; pap:PSPA7_1878; -.
DR   HOGENOM; CLU_019532_2_0_6; -.
DR   OMA; GPILKVN; -.
DR   OrthoDB; 304020at2; -.
DR   Proteomes; UP000001582; 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_1000013701"
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;  46643 MW;  F6EB37766C13D95D CRC64;
     MRAELNQGLI DFLKASPTPF HATASLARRL EAAGYRRLDE RDAWHTEAGG RYYVTRNDSS
     LIAIRLGRRS PLESGFRLVG AHTDSPCLRV KPNPEIARNG FLQLGVEVYG GALFAPWFDR
     DLSLAGRVTF RANGKLESRL VDFRKAIAVI PNLAIHLNRA ANEGWPINAQ NELPPIIAQL
     APGEAADFRL LLDEQLLREH GITADVVLDY ELSFYDTQSA AVIGLNDEFI AGARLDNLLS
     CHAGLEALLN AEGDENCILV CTDHEEVGSC SHCGADGPFL EQVLRRLLPE GDAFSRAIQR
     SLLVSADNAH GVHPNYADRH DANHGPALNG GPVIKINSNQ RYATNSETAG FFRHLCQDSE
     VPVQSFVTRS DMGCGSTIGP ITASQVGVRT VDIGLPTFAM HSIRELAGSH DLAHLVKVLG
     AFYASSELP