ID   APEB_PSEU5              Reviewed;         429 AA.
AC   A4VJG1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=PST_1421;
OS   Pseudomonas stutzeri (strain A1501).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=379731;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A1501;
RX   PubMed=18495935; DOI=10.1073/pnas.0801093105;
RA   Yan Y., Yang J., Dou Y., Chen M., Ping S., Peng J., Lu W., Zhang W.,
RA   Yao Z., Li H., Liu W., He S., Geng L., Zhang X., Yang F., Yu H., Zhan Y.,
RA   Li D., Lin Z., Wang Y., Elmerich C., Lin M., Jin Q.;
RT   "Nitrogen fixation island and rhizosphere competence traits in the genome
RT   of root-associated Pseudomonas stutzeri A1501.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:7564-7569(2008).
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; CP000304; ABP79112.1; -; Genomic_DNA.
DR   RefSeq; WP_011912593.1; NC_009434.1.
DR   AlphaFoldDB; A4VJG1; -.
DR   SMR; A4VJG1; -.
DR   STRING; 379731.PST_1421; -.
DR   MEROPS; M18.002; -.
DR   EnsemblBacteria; ABP79112; ABP79112; PST_1421.
DR   KEGG; psa:PST_1421; -.
DR   eggNOG; COG1362; Bacteria.
DR   HOGENOM; CLU_019532_2_0_6; -.
DR   OMA; GPILKVN; -.
DR   Proteomes; UP000000233; 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;
KW   Reference proteome; Zinc.
FT   CHAIN           1..429
FT                   /note="Probable M18 family aminopeptidase 2"
FT                   /id="PRO_1000013708"
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;  46645 MW;  F98CD5F4B6BC8528 CRC64;
     MRDELNQGLI DYLKASPTPF HATASLAQTL QAAGYKALDE REPWHTEAGG RYYVTRNDSA
     IIAFQLGGKP LAEHGLRLVG AHTDSPCLRV KPQPELQRQG FWQLGVEVYG GALLAPWFDR
     DLSLAGRVTY SRDGRIESQL IDFRQPIACI PNLAIHLNRE ANQGWAINAQ NELPPILAQI
     ASQESPDFRA LLADQLGREH GLVADVVLDF ELSFYDTQPA AVIGLNGDFI AGARLDNLLS
     CFAGLQALFD AGPDETCVLV CTDHEEVGSA SMCGADGPFL EQVLRRLLPE EDDFQRAINR
     SLLISADNAH AVHPNYADKH DGNHGPKLNA GPVIKVNSNQ RYATSSETAG FFRHLCLENE
     VPVQSFVTRS DMGCGSTIGP ITASQLGVRT VDIGLPTFAM HSIRELAGSQ DLAHLVKVLG
     AFYSSAELP