ID   A0A089YSV1_9PSED        Unreviewed;       429 AA.
AC   A0A089YSV1;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Probable M18 family aminopeptidase 2 {ECO:0000256|HAMAP-Rule:MF_00467};
DE            EC=3.4.11.- {ECO:0000256|HAMAP-Rule:MF_00467};
GN   Name=apeB {ECO:0000256|HAMAP-Rule:MF_00467};
GN   ORFNames=LT40_04835 {ECO:0000313|EMBL:AIS16775.1};
OS   Pseudomonas rhizosphaerae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=216142 {ECO:0000313|EMBL:AIS16775.1, ECO:0000313|Proteomes:UP000029499};
RN   [1] {ECO:0000313|EMBL:AIS16775.1, ECO:0000313|Proteomes:UP000029499}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16299 {ECO:0000313|EMBL:AIS16775.1};
RX   PubMed=25483321; DOI=10.1016/j.jbiotec.2014.11.031;
RA   Kwak Y., Jung B.K., Shin J.H.;
RT   "Complete genome sequence of Pseudomonas rhizosphaerae IH5T (=DSM 16299T),
RT   a phosphate-solubilizing rhizobacterium for bacterial biofertilizer.";
RL   J. Biotechnol. 193:137-138(2015).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|HAMAP-Rule:MF_00467, ECO:0000256|RuleBase:RU004387};
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|ARBA:ARBA00008290, ECO:0000256|HAMAP-Rule:MF_00467,
CC       ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; CP009533; AIS16775.1; -; Genomic_DNA.
DR   RefSeq; WP_043187129.1; NZ_CP009533.1.
DR   AlphaFoldDB; A0A089YSV1; -.
DR   STRING; 216142.LT40_04835; -.
DR   KEGG; prh:LT40_04835; -.
DR   eggNOG; COG1362; Bacteria.
DR   HOGENOM; CLU_019532_2_0_6; -.
DR   OrthoDB; 5288740at2; -.
DR   Proteomes; UP000029499; 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   CDD; cd05658; M18_DAP; 1.
DR   Gene3D; 2.30.250.10; Aminopeptidase i, Domain 2; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 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; ASPARTYL AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR28570:SF3; ASPARTYL AMINOPEPTIDASE; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438, ECO:0000256|HAMAP-
KW   Rule:MF_00467};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00467};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00467};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049, ECO:0000256|HAMAP-
KW   Rule:MF_00467};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_00467};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029499};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00467}.
FT   BINDING         82
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00467"
FT   BINDING         156
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00467"
FT   BINDING         401
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00467"
SQ   SEQUENCE   429 AA;  46703 MW;  0D10DEB0340995A6 CRC64;
     MREALNQGLI DFLKASPTPF HATATMARRL EAAGYQRLDE RESWNTVPGG RYYVTRNDSS
     IIAIRLGKHS PLLNGLRMVG AHTDSPCLRV KPQPELQRQG FFQLGVEVYG GALLAPWFDR
     DLSLAGRVTF RRDGKVESQL IDFRLPIAVV PNLAIHLNRE ANQGWAINAQ TELPPVLAQV
     AGDERVDFRA LLTEQLAREH GLNADVVLDY ELSFYDTQSA AVIGLNGDFI AGARLDNLLS
     CYAGLQALLD AEGDESCVLV CTDHEEIGSS SACGADGPML EQVLQRLIPE GDEYVRSIQR
     SLLVSADNAH GVHPNYAEKH DANHGPKLNA GPVIKVNSNQ RYATNSETAG FFRHLCMAVE
     VPVQSFVVRS DMGCGSTIGP ITASHLGVRT VDIGLPTFAM HSIRELAGSQ DLAHLVKVLG
     AFYASSELP
//