FLIG_HELPY
ID FLIG_HELPY Reviewed; 343 AA.
AC O25119;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Flagellar motor switch protein FliG {ECO:0000250|UniProtKB:P0ABZ1, ECO:0000312|EMBL:AAD07420.1};
DE AltName: Full=Flagellar motor switch protein G {ECO:0000312|EMBL:AFV41574.1};
GN Name=fliG {ECO:0000312|EMBL:AFV41574.1};
GN OrderedLocusNames=C694_01785, HP_0352;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1] {ECO:0000312|EMBL:AAD07420.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
RN [2] {ECO:0000312|EMBL:AFV41574.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695 {ECO:0000312|EMBL:AFV41574.1};
RA Manolov A., Prihodko E., Larin A., Karpova I., Semashko T., Alexeev D.,
RA Kostrjukova E., Govorun V.;
RT "Draft genome of Helicobacter pylori.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=SS1 {ECO:0000269|PubMed:10960117};
RX PubMed=10960117; DOI=10.1128/jb.182.18.5274-5277.2000;
RA Allan E., Dorrell N., Foynes S., Anyim M., Wren B.W.;
RT "Mutational analysis of genes encoding the early flagellar components of
RT Helicobacter pylori: evidence for transcriptional regulation of flagellin A
RT biosynthesis.";
RL J. Bacteriol. 182:5274-5277(2000).
RN [4] {ECO:0000305, ECO:0000312|PDB:3USW}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 86-343, FUNCTION, MOTIF, AND
RP MUTAGENESIS OF ARG-209; ARG-217; SER-222; GLU-243 AND GLN-325.
RC STRAIN=ATCC 700392 / 26695 {ECO:0000269|PubMed:22325779};
RX PubMed=22325779; DOI=10.1016/j.str.2011.11.020;
RA Lam K.H., Ip W.S., Lam Y.W., Chan S.O., Ling T.K., Au S.W.;
RT "Multiple conformations of the FliG C-terminal domain provide insight into
RT flagellar motor switching.";
RL Structure 20:315-325(2012).
CC -!- FUNCTION: One of the proteins that forms a switch complex that is
CC proposed to be located at the base of the basal body. This complex
CC interacts with chemotaxis proteins (such as CheY) in addition to
CC contacting components of the motor that determine the direction of
CC flagellar rotation. Required for flagellum synthesis and motility. In
CC H.pylori four flagellar switch proteins are encoded, FliG, FliM, FliN
CC and FliY. {ECO:0000250|UniProtKB:P0ABZ1, ECO:0000269|PubMed:10960117,
CC ECO:0000269|PubMed:22325779, ECO:0000269|PubMed:9252185}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P0ABZ1}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P0ABZ1}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P0ABZ1}. Bacterial flagellum basal body
CC {ECO:0000250|UniProtKB:P0ABZ1}.
CC -!- DISRUPTION PHENOTYPE: Nonflagellate. Forms dense colonies without
CC swarming in contrast to the wild-type which forms diffuse colonies with
CC large, swarming halos. Expression of flagellins FlaA and FlaB and the
CC hook protein FlgE greatly reduced. {ECO:0000269|PubMed:10960117}.
CC -!- SIMILARITY: Belongs to the FliG family. {ECO:0000255}.
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DR EMBL; AE000511; AAD07420.1; -; Genomic_DNA.
DR EMBL; CP003904; AFV41574.1; -; Genomic_DNA.
DR PIR; H64563; H64563.
DR RefSeq; NP_207150.1; NC_000915.1.
DR RefSeq; WP_000201853.1; NC_018939.1.
DR PDB; 3USW; X-ray; 2.60 A; A=86-343.
DR PDB; 3USY; X-ray; 2.71 A; A/B=116-343.
DR PDB; 4FQ0; X-ray; 2.82 A; C/D=116-205.
DR PDB; 5WUJ; X-ray; 2.30 A; B=7-111.
DR PDBsum; 3USW; -.
DR PDBsum; 3USY; -.
DR PDBsum; 4FQ0; -.
DR PDBsum; 5WUJ; -.
DR AlphaFoldDB; O25119; -.
DR SMR; O25119; -.
DR DIP; DIP-3534N; -.
DR IntAct; O25119; 5.
DR MINT; O25119; -.
DR STRING; 85962.C694_01785; -.
DR PaxDb; O25119; -.
DR EnsemblBacteria; AAD07420; AAD07420; HP_0352.
DR KEGG; heo:C694_01785; -.
DR KEGG; hpy:HP_0352; -.
DR PATRIC; fig|85962.47.peg.375; -.
DR eggNOG; COG1536; Bacteria.
DR HOGENOM; CLU_047835_0_0_7; -.
DR OMA; QVRPFEF; -.
DR PhylomeDB; O25119; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0009288; C:bacterial-type flagellum; IMP:UniProtKB.
DR GO; GO:0009425; C:bacterial-type flagellum basal body; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
DR GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IBA:GO_Central.
DR GO; GO:0071978; P:bacterial-type flagellum-dependent swarming motility; IMP:UniProtKB.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR InterPro; IPR000090; Flg_Motor_Flig.
DR InterPro; IPR023087; Flg_Motor_Flig_C.
DR InterPro; IPR011002; FliG_a-hlx.
DR InterPro; IPR032779; FliG_M.
DR InterPro; IPR028263; FliG_N.
DR PANTHER; PTHR30534; PTHR30534; 1.
DR Pfam; PF01706; FliG_C; 1.
DR Pfam; PF14841; FliG_M; 1.
DR Pfam; PF14842; FliG_N; 1.
DR PIRSF; PIRSF003161; FliG; 1.
DR PRINTS; PR00954; FLGMOTORFLIG.
DR SUPFAM; SSF48029; SSF48029; 2.
DR TIGRFAMs; TIGR00207; fliG; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Bacterial flagellum; Cell inner membrane; Cell membrane;
KW Chemotaxis; Flagellar rotation; Membrane; Reference proteome.
FT CHAIN 1..343
FT /note="Flagellar motor switch protein FliG"
FT /id="PRO_0000421839"
FT MOTIF 137..140
FT /note="Part of the EHPQR-motif"
FT MOTIF 245..248
FT /note="M-F-X-F motif; its intrinsic flexibility is probably
FT coupled to flagellar rotation"
FT /evidence="ECO:0000269|PubMed:22325779"
FT SITE 172
FT /note="Part of the EHPQR-motif"
FT MUTAGEN 209
FT /note="R->C: A prominent downward mobility shift in SDS-
FT PAGE and a reduction in the fluorescence intensity upon 5-
FT iodoacetamidofluorescein (5-IAF) haloalkylation after
FT cysteine cross-linking suggest formation of disulfide
FT bonds, hence closeness of corresponding wild-type residues;
FT when associated with C-325."
FT /evidence="ECO:0000269|PubMed:22325779"
FT MUTAGEN 217
FT /note="R->C: A slight downward mobility shift in SDS-PAGE
FT and a reduction in the fluorescence intensity upon 5-
FT iodoacetamidofluorescein (5-IAF) haloalkylation after
FT cysteine cross-linking suggest formation of disulfide
FT bonds, hence closeness of corresponding wild-type residues;
FT when associated with C-325."
FT /evidence="ECO:0000269|PubMed:22325779"
FT MUTAGEN 222
FT /note="S->C: A prominent downward mobility shift in SDS-
FT PAGE and a reduction in the fluorescence intensity upon 5-
FT iodoacetamidofluorescein (5-IAF) haloalkylation after
FT cysteine cross-linking suggest formation of disulfide
FT bonds, hence closeness of corresponding wild-type residues;
FT when associated with C-325."
FT /evidence="ECO:0000269|PubMed:22325779"
FT MUTAGEN 243
FT /note="E->C: A complete upward mobility shift in SDS-PAGE
FT and a reduction in the fluorescence intensity upon 5-
FT iodoacetamidofluorescein (5-IAF) haloalkylation after
FT cysteine cross-linking suggest formation of disulfide
FT bonds, hence closeness of corresponding wild-type residues;
FT when associated with C-325."
FT /evidence="ECO:0000269|PubMed:22325779"
FT MUTAGEN 325
FT /note="Q->C: No mobility shift in SDS-PAGE nor reduction in
FT the fluorescence intensity upon 5-iodoacetamidofluorescein
FT (5-IAF) haloalkylation after cysteine cross-linking. A
FT mobility shift and reduction in the fluorescence intensity
FT after cysteine cross-linking suggest formation of disulfide
FT bonds, hence closeness of corresponding wild-type residues;
FT when associated either with C-209; C-217; C-222 or C-243."
FT /evidence="ECO:0000269|PubMed:22325779"
FT HELIX 8..14
FT /evidence="ECO:0007829|PDB:5WUJ"
FT HELIX 18..29
FT /evidence="ECO:0007829|PDB:5WUJ"
FT HELIX 31..38
FT /evidence="ECO:0007829|PDB:5WUJ"
FT HELIX 43..56
FT /evidence="ECO:0007829|PDB:5WUJ"
FT HELIX 61..77
FT /evidence="ECO:0007829|PDB:5WUJ"
FT HELIX 85..97
FT /evidence="ECO:0007829|PDB:5WUJ"
FT HELIX 99..110
FT /evidence="ECO:0007829|PDB:5WUJ"
FT TURN 116..119
FT /evidence="ECO:0007829|PDB:3USY"
FT HELIX 120..124
FT /evidence="ECO:0007829|PDB:3USW"
FT HELIX 127..134
FT /evidence="ECO:0007829|PDB:3USW"
FT HELIX 139..146
FT /evidence="ECO:0007829|PDB:3USW"
FT HELIX 151..158
FT /evidence="ECO:0007829|PDB:3USW"
FT HELIX 163..173
FT /evidence="ECO:0007829|PDB:3USW"
FT HELIX 181..194
FT /evidence="ECO:0007829|PDB:3USW"
FT HELIX 196..199
FT /evidence="ECO:0007829|PDB:3USY"
FT HELIX 208..216
FT /evidence="ECO:0007829|PDB:3USW"
FT HELIX 220..233
FT /evidence="ECO:0007829|PDB:3USW"
FT HELIX 235..244
FT /evidence="ECO:0007829|PDB:3USW"
FT HELIX 248..253
FT /evidence="ECO:0007829|PDB:3USW"
FT HELIX 256..265
FT /evidence="ECO:0007829|PDB:3USW"
FT HELIX 268..274
FT /evidence="ECO:0007829|PDB:3USW"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:3USW"
FT HELIX 280..288
FT /evidence="ECO:0007829|PDB:3USW"
FT HELIX 292..305
FT /evidence="ECO:0007829|PDB:3USW"
FT HELIX 310..329
FT /evidence="ECO:0007829|PDB:3USW"
SQ SEQUENCE 343 AA; 38326 MW; 861214ED1782980A CRC64;
MATKLTPKQK AQLDELSMSE KIAILLIQVG EDTTGEILRH LDIDSITEIS KQIVQLNGTD
KQIGAAVLEE FFAIFQSNQY INTGGLEYAR ELLTRTLGSE EAKKVMDKLT KSLQTQKNFA
YLGKIKPQQL ADFIINEHPQ TIALILAHME APNAAETLSY FPDEMKAEIS IRMANLGEIS
PQVVKRVSTV LENKLESLTS YKIEVGGLRA VAEIFNRLGQ KSAKTTLARI ESVDNKLAGA
IKEMMFTFED IVKLDNFAIR EILKVADKKD LSLALKTSTK DLTDKFLNNM SSRAAEQFVE
EMQYLGAVKI KDVDVAQRKI IEIVQSLQEK GVIQTGEEED VIE
