ID   APEA_BORBZ              Reviewed;         458 AA.
AC   B7J1T9; Q45055;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=BbuZS7_0368;
OS   Borreliella burgdorferi (strain ZS7) (Borrelia burgdorferi).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=445985;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Wallich R., Kramer M.D., Simon M.M.;
RT   "A Borrelia burgdorferi homolog to the Saccharomyces cerevisiae
RT   aminopeptidase I (APE1).";
RL   Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZS7;
RX   PubMed=20935092; DOI=10.1128/jb.01158-10;
RA   Schutzer S.E., Fraser-Liggett C.M., Casjens S.R., Qiu W.G., Dunn J.J.,
RA   Mongodin E.F., Luft B.J.;
RT   "Whole-genome sequences of thirteen isolates of Borrelia burgdorferi.";
RL   J. Bacteriol. 193:1018-1020(2011).
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; X78708; CAA55361.1; -; Genomic_DNA.
DR   EMBL; CP001205; ACK74892.1; -; Genomic_DNA.
DR   PIR; E70145; E70145.
DR   RefSeq; WP_002657823.1; NC_011728.1.
DR   AlphaFoldDB; B7J1T9; -.
DR   SMR; B7J1T9; -.
DR   EnsemblBacteria; ACK74892; ACK74892; BbuZS7_0368.
DR   GeneID; 56567794; -.
DR   KEGG; bbz:BbuZS7_0368; -.
DR   HOGENOM; CLU_590123_0_0_12; -.
DR   OMA; GPILKVN; -.
DR   OrthoDB; 304020at2; -.
DR   Proteomes; UP000006901; 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_1000125489"
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;  51500 MW;  521BC6DAEF0ABA45 CRC64;
     MKKQNPWIYL NEEEKNQILN FSESYKKFIS KFKTEREVTA YALDKAKKLG FINAEEKKNL
     MPGDKIFYTC REKSVAFAII GKNPIEDGMN FIVSHTDSPR LDAKPSPISE ENELTFIKTN
     YYGGIKKYQW LSTPLSIRGV VFLKNGEKVE INIGDNENDP VFVIPDILPH LDRKIQRNKK
     SDEIVEGENL KILIGSLPIE TKEKNKVKLA TLQLIKEKYK IEEEDFVSSE IEIVPAGTAK
     DVGFDKALIG AYGQDDKICV FTSLESIFDL EETPNKTAIC FLVDKEEIGS TGSTGLDSRY
     LEYFVSDMIF KIKKSEYNNL HVQKALWNSK SISADVCAAI NPLFSSVHDE QNAPQLGYGI
     PIMKYTGHGG KSMASDADAE LVSYIRQLLN KNNIAWQVAT LGKVEEGGGG TVAKFLAGYG
     IRTIDMGPAV ISMHSPMEIT SKFDLYNAYL AYKAFYRE