ID   APEA_BORGP              Reviewed;         458 AA.
AC   Q661Q3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Probable M18 family aminopeptidase 1 {ECO:0000255|HAMAP-Rule:MF_00466};
DE            EC=3.4.11.- {ECO:0000255|HAMAP-Rule:MF_00466};
GN   Name=apeA {ECO:0000255|HAMAP-Rule:MF_00466}; OrderedLocusNames=BG0365;
OS   Borrelia garinii subsp. bavariensis (strain ATCC BAA-2496 / DSM 23469 /
OS   PBi) (Borrelia bavariensis).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=290434;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-2496 / DSM 23469 / PBi;
RX   PubMed=15547252; DOI=10.1093/nar/gkh953;
RA   Gloeckner G., Lehmann R., Romualdi A., Pradella S., Schulte-Spechtel U.,
RA   Schilhabel M., Wilske B., Suehnel J., Platzer M.;
RT   "Comparative analysis of the Borrelia garinii genome.";
RL   Nucleic Acids Res. 32:6038-6046(2004).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00466};
CC   -!- SIMILARITY: Belongs to the peptidase M18 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00466}.
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DR   EMBL; CP000013; AAU07218.1; -; Genomic_DNA.
DR   RefSeq; WP_011193692.1; NC_006156.1.
DR   AlphaFoldDB; Q661Q3; -.
DR   SMR; Q661Q3; -.
DR   STRING; 290434.BG0365; -.
DR   EnsemblBacteria; AAU07218; AAU07218; BG0365.
DR   KEGG; bga:BG0365; -.
DR   eggNOG; COG1362; Bacteria.
DR   HOGENOM; CLU_590123_0_0_12; -.
DR   OMA; GPILKVN; -.
DR   OrthoDB; 304020at2; -.
DR   Proteomes; UP000002276; 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_00466; Aminopeptidase_M18_1; 1.
DR   InterPro; IPR022983; M18_aminopeptidase_1.
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..458
FT                   /note="Probable M18 family aminopeptidase 1"
FT                   /id="PRO_1000013696"
FT   BINDING         95
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00466"
FT   BINDING         170
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00466"
FT   BINDING         434
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00466"
SQ   SEQUENCE   458 AA;  51268 MW;  3E5E36188160786C CRC64;
     MKKQNPWISL SEEEKNQIFN FSESYKKFIS KFKTEREVTS YALDKAKKRG FIDAEEKKNL
     IPGDKIFYTC REKSVAFAII GKNPIENGMN LIVSHTDSPR LDAKPSPISE ENELAFLKTN
     YYGGIKKYQW LSTPLSIRGV VFLKNGEKVE INIGDNENDP VFVIPDILPH LDKKIQRNKK
     SDEIIEGENL KILIGSLPIE SKEQDKVKLG TLQLIKEKYK IEEEDFVSSE IEIVPAGTAK
     DVGFDKALIG AYGQDDKICA YASLEAIFDL EEIPSKTAIC FLVDKEEIGS TGSTGLDSRY
     LEYFVSDMIF KIKKSEYNNL QVQKALWNSK SISADVCAAI NPIFNSVHDA QNAPKLGYGI
     PIMKYTGHGG KVMASDADAE LVSYIRQLLN KNNIAWQVAT LGKVEEGGGG TVAKFLASYG
     IRTIDMGPAV ISMHSPMEIT SKFDLYNAYL AYKAFYKE