FLHC_CUPPJ
ID FLHC_CUPPJ Reviewed; 210 AA.
AC Q46TH1;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Flagellar transcriptional regulator FlhC {ECO:0000255|HAMAP-Rule:MF_01891};
GN Name=flhC {ECO:0000255|HAMAP-Rule:MF_01891}; OrderedLocusNames=Reut_B4210;
OS Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS (strain JMP 134)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=264198;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMP134 / LMG 1197;
RX PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA Kyrpides N.C.;
RT "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT versatile pollutant degrader.";
RL PLoS ONE 5:E9729-E9729(2010).
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:0000255|HAMAP-Rule:MF_01891}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01891};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01891};
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. {ECO:0000255|HAMAP-
CC Rule:MF_01891}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01891}.
CC -!- SIMILARITY: Belongs to the FlhC family. {ECO:0000255|HAMAP-
CC Rule:MF_01891}.
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DR EMBL; CP000091; AAZ63563.1; -; Genomic_DNA.
DR RefSeq; WP_011300329.1; NC_007348.1.
DR AlphaFoldDB; Q46TH1; -.
DR SMR; Q46TH1; -.
DR STRING; 264198.Reut_B4210; -.
DR EnsemblBacteria; AAZ63563; AAZ63563; Reut_B4210.
DR KEGG; reu:Reut_B4210; -.
DR eggNOG; ENOG502Z927; Bacteria.
DR HOGENOM; CLU_122824_0_0_4; -.
DR OMA; WRPNAHA; -.
DR OrthoDB; 1247512at2; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0045893; P:positive regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:1902208; P:regulation of bacterial-type flagellum assembly; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01891; FhlC; 1.
DR InterPro; IPR007944; FlhC.
DR Pfam; PF05280; FlhC; 1.
DR PIRSF; PIRSF003159; FlhC; 1.
PE 3: Inferred from homology;
KW Activator; Bacterial flagellum biogenesis; Cytoplasm; DNA-binding;
KW Metal-binding; Transcription; Transcription regulation; Zinc.
FT CHAIN 1..210
FT /note="Flagellar transcriptional regulator FlhC"
FT /id="PRO_0000406759"
FT BINDING 144
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01891"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01891"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01891"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01891"
SQ SEQUENCE 210 AA; 23112 MW; DAA1EB77BACA3412 CRC64;
MKTTAQTAPA RSALQDASDT QLAIELIGLG ARPQVVEAEV TLSRSRVYRL YRELTGGSPP
KGMLPFSADW FVTWRPNAHA SYLLSVHEYM QQRAGLPGIR AVLNSYRVYA EHMKANNEEC
LISFTRFWTL VRFCEGGLLQ LSTCPCCGGR FVTHAHEPLA SFICTLCQPP SRVRRSVRRE
TPHATANAPA AVLGNRPPVA MPGFGMVPAL