ID   APEB_PSEAB              Reviewed;         429 AA.
AC   Q02Q78;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=PA14_21990;
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14;
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA   Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(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; CP000438; ABJ12496.1; -; Genomic_DNA.
DR   RefSeq; WP_003091583.1; NZ_CP034244.1.
DR   AlphaFoldDB; Q02Q78; -.
DR   SMR; Q02Q78; -.
DR   PRIDE; Q02Q78; -.
DR   EnsemblBacteria; ABJ12496; ABJ12496; PA14_21990.
DR   KEGG; pau:PA14_21990; -.
DR   HOGENOM; CLU_019532_2_0_6; -.
DR   OMA; GPILKVN; -.
DR   BioCyc; PAER208963:G1G74-1827-MON; -.
DR   Proteomes; UP000000653; 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_1000013702"
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;  46601 MW;  26D547C941ED558B CRC64;
     MRAELNQGLI DFLKASPTPF HATASLARRL EAAGYRRLDE RDAWHTEAGG RYYVTRNDSS
     LIAIRLGRRS PLESGFRLVG AHTDSPCLRV KPNPEIARNG FLQLGVEVYG GALFAPWFDR
     DLSLAGRVTF RANGKLESRL VDFRKAIAVI PNLAIHLNRA ANEGWPINAQ NELPPIIAQL
     APGEAADFRL LLDEQLLREH GITADVVLDY ELSFYDTQSA AVVGLNDEFI AGARLDNLLS
     CHAGLEALLN AEGDENCILV CTDHEEVGSC SHCGADGPFL EQVLRRLLPE GDAFSRAIQR
     SLLVSADNAH GVHPNYADKH DANHGPALNG GPVIKINSNQ RYATNSETAG FFRHLCQDSE
     VPVQSFVTRS DMGCGSTIGP ITASQVGVRT VDIGLPTFAM HSIRELAGSH DLAHLVKVLG
     AFYASSELP