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 27-MAR-2024, entry version 124.
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; Spirochaetota; Spirochaetia; Spirochaetales; Borreliaceae;
OC 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 PATRIC; fig|224326.49.peg.1017; -.
DR OrthoDB; 9764268at2; -.
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; 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; 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
//
