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FLII_BORBU
ID   FLII_BORBU              Reviewed;         436 AA.
AC   P52607; Q44913; Q44916;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 153.
DE   RecName: Full=Flagellum-specific ATP synthase;
DE            EC=7.1.2.2;
GN   Name=fliI; OrderedLocusNames=BB_0288;
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 [GENOMIC DNA].
RC   STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RA   Dunn J.J., Butler-Loffredo L., Kieleczawa J., Medalle J., Luft B.J.;
RL   Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=212;
RX   PubMed=8626068; DOI=10.1016/0378-1119(95)00743-1;
RA   Ge Y., Old I.G., Saint-Girons I., Yelton D.B., Charon N.W.;
RT   "FliH and fliI of Borrelia burgdorferi are similar to flagellar and
RT   virulence factor export proteins of other bacteria.";
RL   Gene 168:73-75(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=212;
RA   Ge Y., Saint-Girons I., Old I.G., Charon N.W.;
RL   Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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   -!- FUNCTION: Probable catalytic subunit of a protein translocase for
CC       flagellum-specific export, or a proton translocase involved in local
CC       circuits at the flagellum. May be involved in a specialized protein
CC       export pathway that proceeds without signal peptide cleavage.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate;
CC         Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000305}.
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DR   EMBL; U43739; AAA85611.1; -; Genomic_DNA.
DR   EMBL; L43325; AAB04681.1; -; Genomic_DNA.
DR   EMBL; L76303; AAB51413.1; -; Genomic_DNA.
DR   EMBL; AE000783; AAC66660.1; -; Genomic_DNA.
DR   PIR; H70135; H70135.
DR   RefSeq; NP_212422.1; NC_001318.1.
DR   RefSeq; WP_002660657.1; NC_001318.1.
DR   AlphaFoldDB; P52607; -.
DR   SMR; P52607; -.
DR   STRING; 224326.BB_0288; -.
DR   PRIDE; P52607; -.
DR   EnsemblBacteria; AAC66660; AAC66660; BB_0288.
DR   KEGG; bbu:BB_0288; -.
DR   PATRIC; fig|224326.49.peg.687; -.
DR   HOGENOM; CLU_022398_5_1_12; -.
DR   OMA; MLMMDSV; -.
DR   Proteomes; UP000001807; Chromosome.
DR   GO; GO:0009288; C:bacterial-type flagellum; IEA:InterPro.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030257; C:type III protein secretion system complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-EC.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
DR   GO; GO:0044781; P:bacterial-type flagellum organization; IEA:UniProtKB-KW.
DR   GO; GO:0030254; P:protein secretion by the type III secretion system; IEA:InterPro.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR   InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR   InterPro; IPR005714; ATPase_T3SS_FliI/YscN.
DR   InterPro; IPR022426; FliI_clade3.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR040627; T3SS_ATPase_C.
DR   Pfam; PF00006; ATP-synt_ab; 1.
DR   Pfam; PF02874; ATP-synt_ab_N; 1.
DR   Pfam; PF18269; T3SS_ATPase_C; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR03498; FliI_clade3; 1.
DR   TIGRFAMs; TIGR01026; fliI_yscN; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; ATP-binding; Bacterial flagellum biogenesis;
KW   Bacterial flagellum protein export; Cytoplasm; Hydrogen ion transport;
KW   Ion transport; Nucleotide-binding; Protein transport; Reference proteome;
KW   Translocase; Transport.
FT   CHAIN           1..436
FT                   /note="Flagellum-specific ATP synthase"
FT                   /id="PRO_0000144689"
FT   BINDING         165..172
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        76
FT                   /note="S -> N (in Ref. 2; AAB04681 and 3; AAB51413)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        118
FT                   /note="L -> F (in Ref. 2; AAB04681)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        128
FT                   /note="E -> Q (in Ref. 2; AAB04681)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        158..167
FT                   /note="GQRVGIFSGS -> RTKELVFFWF (in Ref. 2; AAB04681)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        171..174
FT                   /note="KSTL -> NSYLC (in Ref. 2; AAB04681)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        251
FT                   /note="Missing (in Ref. 2; AAB04681)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        252..253
FT                   /note="LL -> FC (in Ref. 2; AAB04681 and 3; AAB51413)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        259
FT                   /note="R -> W (in Ref. 2; AAB04681)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        265..274
FT                   /note="REMSLSLGEP -> KRDVSFFRGA (in Ref. 2; AAB04681)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        322
FT                   /note="A -> D (in Ref. 2; AAB04681)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   436 AA;  48382 MW;  F97F8829E8EBFF1C CRC64;
     MSNFFENYLR QVDDIETVSF VGRVQKIKGL LVESLGPQCA IGDLCLIDQR NGKKVCAEVL
     GFNGPYVSLM AYEGFSGIEV GNKVYSLNKG LEINLSDELL GRVIDSLGRP IDNKGSFLNN
     SYKELIFEKI NPINRSIFED QILTGVKVLD GFLPVAKGQR VGIFSGSGVG KSTLLGMIAK
     NSNADVNVIA FIGERGRELN EFIEHELGEE RLKKSVLVVS TSDESPISRY KGAYVATMIA
     EYFREQGKDV ALLFDSITRF ANAKREMSLS LGEPPVAKGY PPSVFVEIPI LLERSGFNGN
     GGSVTGFYTV LVEGDDFTEP VADNIKAVLD GHIILDRDLF DRGIYPSINV LSSTSRSIHR
     IMSLEKQKLI MKARNLLSIY KDYEDLIRTG IYLKGSNKDV DFAISKYPKI INFISQGINE
     TFDFENLEDE IKEILS
 
 
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