FLHC_ECOLI
ID FLHC_ECOLI Reviewed; 192 AA.
AC P0ABY7; P11165; P76303;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Flagellar transcriptional regulator FlhC;
GN Name=flhC; Synonyms=flaI; OrderedLocusNames=b1891, JW1880;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2832369; DOI=10.1128/jb.170.4.1575-1581.1988;
RA Bartlett D.H., Frantz B.B., Matsumura P.;
RT "Flagellar transcriptional activators FlbB and FlaI: gene sequences and 5'
RT consensus sequences of operons under FlbB and FlaI control.";
RL J. Bacteriol. 170:1575-1581(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION, INTERACTION WITH FLHD, AND DNA-BINDING.
RC STRAIN=K12 / MC1000 / ATCC 39531;
RX PubMed=7961507; DOI=10.1128/jb.176.23.7345-7351.1994;
RA Liu X., Matsumura P.;
RT "The FlhD/FlhC complex, a transcriptional activator of the Escherichia coli
RT flagellar class II operons.";
RL J. Bacteriol. 176:7345-7351(1994).
RN [6]
RP INDUCTION.
RC STRAIN=K12;
RX PubMed=7642497; DOI=10.1128/jb.177.16.4696-4702.1995;
RA Shin S., Park C.;
RT "Modulation of flagellar expression in Escherichia coli by acetyl phosphate
RT and the osmoregulator OmpR.";
RL J. Bacteriol. 177:4696-4702(1995).
RN [7]
RP INDUCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=10601207; DOI=10.1128/jb.181.24.7500-7508.1999;
RA Soutourina O., Kolb A., Krin E., Laurent-Winter C., Rimsky S., Danchin A.,
RA Bertin P.;
RT "Multiple control of flagellum biosynthesis in Escherichia coli: role of H-
RT NS protein and the cyclic AMP-catabolite activator protein complex in
RT transcription of the flhDC master operon.";
RL J. Bacteriol. 181:7500-7508(1999).
RN [8]
RP FUNCTION, AND INTERACTION WITH FLHD.
RC STRAIN=K12 / YK410;
RX PubMed=11169100; DOI=10.1046/j.1365-2958.2001.02248.x;
RA Campos A., Matsumura P.;
RT "Extensive alanine scanning reveals protein-protein and protein-DNA
RT interaction surfaces in the global regulator FlhD from Escherichia coli.";
RL Mol. Microbiol. 39:581-594(2001).
RN [9]
RP INDUCTION.
RC STRAIN=K12;
RX PubMed=11929534; DOI=10.1046/j.1365-2958.2002.02803.x;
RA Sperandio V., Torres A.G., Kaper J.B.;
RT "Quorum sensing Escherichia coli regulators B and C (QseBC): a novel two-
RT component regulatory system involved in the regulation of flagella and
RT motility by quorum sensing in E. coli.";
RL Mol. Microbiol. 43:809-821(2002).
RN [10]
RP FUNCTION, AND DNA-BINDING.
RC STRAIN=K12 / MC1000 / ATCC 39531;
RX PubMed=15941987; DOI=10.1099/mic.0.27879-0;
RA Stafford G.P., Ogi T., Hughes C.;
RT "Binding and transcriptional activation of non-flagellar genes by the
RT Escherichia coli flagellar master regulator FlhD2C2.";
RL Microbiology 151:1779-1788(2005).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), SUBUNIT, AND ZINC-BINDING.
RX PubMed=16337229; DOI=10.1016/j.jmb.2005.11.020;
RA Wang S., Fleming R.T., Westbrook E.M., Matsumura P., McKay D.B.;
RT "Structure of the Escherichia coli FlhDC complex, a prokaryotic heteromeric
RT regulator of transcription.";
RL J. Mol. Biol. 355:798-808(2006).
CC -!- FUNCTION: Functions in complex with FlhD as a master transcriptional
CC regulator that regulates transcription of several flagellar and non-
CC flagellar operons by binding to their promoter region. Activates
CC expression of class 2 flagellar genes, including fliA, which is a
CC flagellum-specific sigma factor that turns on the class 3 genes. Also
CC regulates genes whose products function in a variety of physiological
CC pathways. {ECO:0000269|PubMed:11169100, ECO:0000269|PubMed:15941987,
CC ECO:0000269|PubMed:7961507}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000305};
CC -!- SUBUNIT: Heterohexamer composed of two FlhC and four FlhD subunits.
CC Each FlhC binds a FlhD dimer, forming a heterotrimer, and a hexamer
CC assembles by dimerization of two heterotrimers.
CC {ECO:0000269|PubMed:16337229}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Expression is regulated by a large number of systems,
CC including induction by quorum sensing via the two-component regulatory
CC system QseB/QseC, induction by cAMP-CRP, repression by high osmolarity
CC via OmpR and repression by H-NS. {ECO:0000269|PubMed:10601207,
CC ECO:0000269|PubMed:11929534, ECO:0000269|PubMed:7642497}.
CC -!- SIMILARITY: Belongs to the FlhC family. {ECO:0000305}.
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DR EMBL; M19439; AAA23788.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74961.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15712.1; -; Genomic_DNA.
DR PIR; C64952; XMECIF.
DR RefSeq; NP_416405.1; NC_000913.3.
DR RefSeq; WP_001291603.1; NZ_STEB01000026.1.
DR PDB; 2AVU; X-ray; 3.00 A; E/F=1-192.
DR PDBsum; 2AVU; -.
DR AlphaFoldDB; P0ABY7; -.
DR SMR; P0ABY7; -.
DR BioGRID; 4262244; 9.
DR ComplexPortal; CPX-2508; FlhDC transcriptional regulation complex.
DR DIP; DIP-9645N; -.
DR IntAct; P0ABY7; 1.
DR STRING; 511145.b1891; -.
DR PaxDb; P0ABY7; -.
DR PRIDE; P0ABY7; -.
DR EnsemblBacteria; AAC74961; AAC74961; b1891.
DR EnsemblBacteria; BAA15712; BAA15712; BAA15712.
DR GeneID; 58391140; -.
DR GeneID; 947280; -.
DR KEGG; ecj:JW1880; -.
DR KEGG; eco:b1891; -.
DR PATRIC; fig|1411691.4.peg.356; -.
DR EchoBASE; EB0315; -.
DR eggNOG; ENOG502Z927; Bacteria.
DR HOGENOM; CLU_122824_0_0_6; -.
DR OMA; MLQLSAC; -.
DR PhylomeDB; P0ABY7; -.
DR BioCyc; EcoCyc:MON0-2488; -.
DR EvolutionaryTrace; P0ABY7; -.
DR PRO; PR:P0ABY7; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005667; C:transcription regulator complex; IPI:ComplexPortal.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0044781; P:bacterial-type flagellum organization; IEA:UniProtKB-KW.
DR GO; GO:1902210; P:positive regulation of bacterial-type flagellum assembly; IDA:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:ComplexPortal.
DR GO; GO:0006351; P:transcription, DNA-templated; IDA:EcoCyc.
DR HAMAP; MF_01891; FhlC; 1.
DR InterPro; IPR007944; FlhC.
DR Pfam; PF05280; FlhC; 1.
DR PIRSF; PIRSF003159; FlhC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Bacterial flagellum biogenesis; Cytoplasm;
KW DNA-binding; Metal-binding; Reference proteome; Transcription;
KW Transcription regulation; Zinc.
FT CHAIN 1..192
FT /note="Flagellar transcriptional regulator FlhC"
FT /id="PRO_0000064337"
FT BINDING 137
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 160
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT CONFLICT 149
FT /note="H -> D (in Ref. 1; AAA23788)"
FT /evidence="ECO:0000305"
FT HELIX 6..21
FT /evidence="ECO:0007829|PDB:2AVU"
FT HELIX 27..32
FT /evidence="ECO:0007829|PDB:2AVU"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:2AVU"
FT HELIX 37..47
FT /evidence="ECO:0007829|PDB:2AVU"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:2AVU"
FT HELIX 62..65
FT /evidence="ECO:0007829|PDB:2AVU"
FT HELIX 68..85
FT /evidence="ECO:0007829|PDB:2AVU"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:2AVU"
FT HELIX 92..105
FT /evidence="ECO:0007829|PDB:2AVU"
FT HELIX 117..128
FT /evidence="ECO:0007829|PDB:2AVU"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:2AVU"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:2AVU"
FT STRAND 143..149
FT /evidence="ECO:0007829|PDB:2AVU"
SQ SEQUENCE 192 AA; 21566 MW; 4504AF0580545C0C CRC64;
MSEKSIVQEA RDIQLAMELI TLGARLQMLE SETQLSRGRL IKLYKELRGS PPPKGMLPFS
TDWFMTWEQN VHASMFCNAW QFLLKTGLCN GVDAVIKAYR LYLEQCPQAE EGPLLALTRA
WTLVRFVESG LLQLSSCNCC GGNFITHAHQ PVGSFACSLC QPPSRAVKRR KLSQNPADII
PQLLDEQRVQ AV
