ID   APEA_BORAP              Reviewed;         458 AA.
AC   Q0SNE8; G0IS10;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 95.
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};
GN   OrderedLocusNames=BAPKO_0374, BafPKo_0365;
OS   Borreliella afzelii (strain PKo) (Borrelia afzelii).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=390236;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PKo;
RX   PubMed=16914037; DOI=10.1186/1471-2164-7-211;
RA   Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M., Suehnel J.,
RA   Wilske B., Platzer M.;
RT   "Comparative genome analysis: selection pressure on the Borrelia vls
RT   cassettes is essential for infectivity.";
RL   BMC Genomics 7:211-211(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PKo;
RX   PubMed=22123755; DOI=10.1128/jb.05951-11;
RA   Casjens S.R., Mongodin E.F., Qiu W.G., Dunn J.J., Luft B.J.,
RA   Fraser-Liggett C.M., Schutzer S.E.;
RT   "Whole-genome sequences of two Borrelia afzelii and two Borrelia garinii
RT   Lyme disease agent isolates.";
RL   J. Bacteriol. 193:6995-6996(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000395; ABH01630.1; -; Genomic_DNA.
DR   EMBL; CP002933; AEL69591.1; -; Genomic_DNA.
DR   RefSeq; WP_004790261.1; NC_017238.1.
DR   AlphaFoldDB; Q0SNE8; -.
DR   SMR; Q0SNE8; -.
DR   STRING; 390236.BafPKo_0365; -.
DR   EnsemblBacteria; AEL69591; AEL69591; BafPKo_0365.
DR   KEGG; baf:BAPKO_0374; -.
DR   KEGG; bafz:BafPKo_0365; -.
DR   PATRIC; fig|390236.22.peg.358; -.
DR   eggNOG; COG1362; Bacteria.
DR   HOGENOM; CLU_590123_0_0_12; -.
DR   OMA; GPILKVN; -.
DR   OrthoDB; 304020at2; -.
DR   Proteomes; UP000005216; 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_1000013695"
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;  51478 MW;  8A3C6E5773BFAFBB CRC64;
     MKKQNPWISL SEEEKNQIFN FSENYKKFIS KFKTEREVAS YALDKAKKKG FLNAEEKKNL
     MPGDKIFYTC REKTVAFAII GKNPIENGMN LIVSHTDSPR LDAKPSPISE ENELVFLKTN
     YYGGIKKYQW LSTPLSIRGV IFLKNGEKVE INIGDNENDP VFIIPDILPH LDRKIQRNKK
     SDEIIEGENL KILIGSLPIE TKEKNKVKLA TLQLIKEKYK IEEEDFVSSE IEIVPAGTAK
     DVGFDKALIG AYGQDDKICV YTSLESIFDL EEIPNKTAIC FLVDKEEIGS TGSTGLDSRY
     LEYFVSDMIF KIKKSEYNNL HVQKALWNSK SISADVCAAI NPLFSSVHDE QNAPKLGYGI
     PIMKYTGHGG KSMASDADAE LVSYIRQLLN KNNIAWQVAT LGKVEEGGGG TVAKFLAGYG
     IRTIDMGPAV ISMHSPMEIT SKFDLYNAYL AYKAFYKE