ID   APEB_BORBU              Reviewed;         423 AA.
AC   O51572;
DT   24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Probable M18 family aminopeptidase 2;
DE            EC=3.4.11.-;
GN   Name=apeB; OrderedLocusNames=BB_0627;
OS   Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS   (Borrelia burgdorferi).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=224326;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX   PubMed=9403685; DOI=10.1038/37551;
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA   Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA   Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA   van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA   Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA   Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA   Smith H.O., Venter J.C.;
RT   "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL   Nature 390:580-586(1997).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the peptidase M18 family. {ECO:0000305}.
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DR   EMBL; AE000783; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; B70178; B70178.
DR   RefSeq; WP_023003298.1; NC_001318.1.
DR   RefSeq; YP_008686584.1; NC_001318.1.
DR   PRIDE; O51572; -.
DR   PATRIC; fig|224326.49.peg.1017; -.
DR   OMA; KSGCHAI; -.
DR   Proteomes; UP000001807; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:CAFA.
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..423
FT                   /note="Probable M18 family aminopeptidase 2"
FT                   /id="PRO_0000173460"
FT   BINDING         84
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
FT   BINDING         157
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
FT   BINDING         397
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   423 AA;  47381 MW;  BE62EEF05A2B100B CRC64;
     MVXXKTLEPK FFQSLLDNSP TPYHLVNYIE EKLINYFNAQ QLKLNEKWKI KTGSYYIKKE
     GTSLIAFNID VKKKYEPFLI AAAHTDSPGL KLKIDATEKV SGVFYNHIEV YGSPIISTWI
     DRDLSLAGIV YFKKNENIES KLINIENIGI IPNLAIHLNR QINEGFKYNA HDNLTVISST
     KKAIKDNILE QLGIECENFL SCDLIFTESQ PSKIIGTEGE FLASKNLDNK SGCHAIMNSY
     VHTSNDKNKI AVFFDNEEVG SLTSRGADSN FLSEVLERID IALDLTREEH LIKTNKSFNI
     SIDSVHGIHP GYTSKHDPNY QANLGKGVVV KNSANFRYAT TSTGFAKLKN LAIKNNIKIQ
     EIIMKANVPS GTTIGPISNA RTGIETIDIG TPMWAMHSLR ETVSIADHIE AIKLLRAFFE
     KGI