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FLIA_ECOLI
ID   FLIA_ECOLI              Reviewed;         239 AA.
AC   P0AEM6; P31804;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=RNA polymerase sigma factor FliA {ECO:0000255|HAMAP-Rule:MF_00962};
DE   AltName: Full=RNA polymerase sigma factor for flagellar operon {ECO:0000255|HAMAP-Rule:MF_00962};
DE   AltName: Full=Sigma F {ECO:0000255|HAMAP-Rule:MF_00962};
DE   AltName: Full=Sigma-27;
DE   AltName: Full=Sigma-28 {ECO:0000255|HAMAP-Rule:MF_00962};
GN   Name=fliA {ECO:0000255|HAMAP-Rule:MF_00962}; Synonyms=flaD, rpoF;
GN   OrderedLocusNames=b1922, JW1907;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=K12;
RX   PubMed=7590326; DOI=10.1016/0378-1119(95)00480-t;
RA   Liu X., Matsumura P.;
RT   "An alternative sigma factor controls transcription of flagellar class-III
RT   operons in Escherichia coli: gene sequence, overproduction, purification
RT   and characterization.";
RL   Gene 164:81-84(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12 / RP437;
RX   PubMed=8550423; DOI=10.1128/jb.178.1.24-34.1996;
RA   Mytelka D.S., Chamberlin M.J.;
RT   "Escherichia coli fliAZY operon.";
RL   J. Bacteriol. 178:24-34(1996).
RN   [3]
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   [4]
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   [5]
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   [6]
RP   FUNCTION.
RX   PubMed=3536871; DOI=10.1128/jb.168.3.1315-1318.1986;
RA   Komeda Y.;
RT   "Transcriptional control of flagellar genes in Escherichia coli K-12.";
RL   J. Bacteriol. 168:1315-1318(1986).
RN   [7]
RP   FUNCTION.
RX   PubMed=2644646; DOI=10.1073/pnas.86.3.830;
RA   Arnosti D.N., Chamberlin M.J.;
RT   "Secondary sigma factor controls transcription of flagellar and chemotaxis
RT   genes in Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:830-834(1989).
RN   [8]
RP   FUNCTION.
RX   PubMed=8866483; DOI=10.1111/j.1365-2958.1996.tb02569.x;
RA   Liu X., Matsumura P.;
RT   "Differential regulation of multiple overlapping promoters in flagellar
RT   class II operons in Escherichia coli.";
RL   Mol. Microbiol. 21:613-620(1996).
RN   [9]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=16397770; DOI=10.1007/s00253-005-0263-8;
RA   Wood T.K., Gonzalez Barrios A.F., Herzberg M., Lee J.;
RT   "Motility influences biofilm architecture in Escherichia coli.";
RL   Appl. Microbiol. Biotechnol. 72:361-367(2006).
RN   [10]
RP   MUTAGENESIS OF GLN-73; ARG-74; ALA-78; ASP-81; ARG-84; ARG-91; SER-92;
RP   ARG-94; ARG-95; ASN-96 AND ARG-98.
RX   PubMed=19400790; DOI=10.1111/j.1365-2958.2009.06691.x;
RA   Koo B.M., Rhodius V.A., Campbell E.A., Gross C.A.;
RT   "Mutational analysis of Escherichia coli sigma28 and its target promoters
RT   reveals recognition of a composite -10 region, comprised of an 'extended
RT   -10' motif and a core -10 element.";
RL   Mol. Microbiol. 72:830-843(2009).
CC   -!- FUNCTION: Sigma factors are initiation factors that promote the
CC       attachment of RNA polymerase to specific initiation sites and are then
CC       released. This sigma factor controls the expression of flagella-related
CC       genes. {ECO:0000255|HAMAP-Rule:MF_00962, ECO:0000269|PubMed:2644646,
CC       ECO:0000269|PubMed:3536871, ECO:0000269|PubMed:7590326,
CC       ECO:0000269|PubMed:8866483}.
CC   -!- INTERACTION:
CC       P0AEM6; P0AEM4: flgM; NbExp=4; IntAct=EBI-549807, EBI-1121952;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00962}.
CC   -!- DOMAIN: The sigma-70 factor domain-2 mediates sequence-specific
CC       interaction with the -10 element in promoter DNA, and plays an
CC       important role in melting the double-stranded DNA and the formation of
CC       the transcription bubble. The sigma-70 factor domain-2 mediates
CC       interaction with the RNA polymerase subunits RpoB and RpoC (By
CC       similarity). {ECO:0000250}.
CC   -!- DOMAIN: The sigma-70 factor domain-4 contains a helix-turn-helix (H-T-
CC       H) motif that mediates interaction with the -35 element in promoter
CC       DNA. The domain also mediates interaction with the RNA polymerase
CC       subunit RpoA (By similarity). {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Mutants have poor biofilms (decrease in biomass,
CC       surface coverage and mean thickness). {ECO:0000269|PubMed:16397770}.
CC   -!- MISCELLANEOUS: The distinguishing feature of FliA promoters is a long
CC       -10 region (GCCGATAA). The upstream GC constitutes an extended -10
CC       motif and is recognized by Arg-91 (PubMed:19400790).
CC       {ECO:0000305|PubMed:19400790}.
CC   -!- SIMILARITY: Belongs to the sigma-70 factor family. FliA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00962}.
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DR   EMBL; L36677; AAC37011.1; -; Genomic_DNA.
DR   EMBL; U18539; AAC43543.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC74989.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA15742.1; -; Genomic_DNA.
DR   PIR; JC4346; JC4346.
DR   RefSeq; NP_416432.3; NC_000913.3.
DR   RefSeq; WP_001087467.1; NZ_SSZK01000069.1.
DR   PDB; 6PMI; EM; 3.86 A; F=1-239.
DR   PDB; 6PMJ; EM; 3.91 A; F=1-239.
DR   PDBsum; 6PMI; -.
DR   PDBsum; 6PMJ; -.
DR   AlphaFoldDB; P0AEM6; -.
DR   SMR; P0AEM6; -.
DR   BioGRID; 4259656; 28.
DR   BioGRID; 853104; 3.
DR   ComplexPortal; CPX-4886; DNA-directed RNA polymerase holoenzyme complex, SigmaF variant.
DR   DIP; DIP-47959N; -.
DR   IntAct; P0AEM6; 21.
DR   STRING; 511145.b1922; -.
DR   PaxDb; P0AEM6; -.
DR   PRIDE; P0AEM6; -.
DR   EnsemblBacteria; AAC74989; AAC74989; b1922.
DR   EnsemblBacteria; BAA15742; BAA15742; BAA15742.
DR   GeneID; 66674188; -.
DR   GeneID; 948824; -.
DR   KEGG; ecj:JW1907; -.
DR   KEGG; eco:b1922; -.
DR   PATRIC; fig|1411691.4.peg.327; -.
DR   EchoBASE; EB1330; -.
DR   eggNOG; COG1191; Bacteria.
DR   HOGENOM; CLU_014793_8_1_6; -.
DR   InParanoid; P0AEM6; -.
DR   OMA; IKFETYA; -.
DR   PhylomeDB; P0AEM6; -.
DR   BioCyc; EcoCyc:EG11355-MON; -.
DR   BioCyc; MetaCyc:EG11355-MON; -.
DR   PRO; PR:P0AEM6; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0000345; C:cytosolic DNA-directed RNA polymerase complex; IPI:ComplexPortal.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:InterPro.
DR   GO; GO:0016987; F:sigma factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0044780; P:bacterial-type flagellum assembly; IC:ComplexPortal.
DR   GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IC:ComplexPortal.
DR   GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:UniProtKB-UniRule.
DR   GO; GO:2000142; P:regulation of DNA-templated transcription, initiation; IDA:ComplexPortal.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR   HAMAP; MF_00962; Sigma70_FliA; 1.
DR   InterPro; IPR014284; RNA_pol_sigma-70_dom.
DR   InterPro; IPR000943; RNA_pol_sigma70.
DR   InterPro; IPR007627; RNA_pol_sigma70_r2.
DR   InterPro; IPR007624; RNA_pol_sigma70_r3.
DR   InterPro; IPR007630; RNA_pol_sigma70_r4.
DR   InterPro; IPR012845; RNA_pol_sigma_FliA_WhiG.
DR   InterPro; IPR013325; RNA_pol_sigma_r2.
DR   InterPro; IPR013324; RNA_pol_sigma_r3/r4-like.
DR   InterPro; IPR028617; Sigma70_FliA.
DR   Pfam; PF04542; Sigma70_r2; 1.
DR   Pfam; PF04539; Sigma70_r3; 1.
DR   Pfam; PF04545; Sigma70_r4; 1.
DR   PIRSF; PIRSF000770; RNA_pol_sigma-SigE/K; 1.
DR   PRINTS; PR00046; SIGMA70FCT.
DR   SUPFAM; SSF88659; SSF88659; 2.
DR   SUPFAM; SSF88946; SSF88946; 1.
DR   TIGRFAMs; TIGR02479; FliA_WhiG; 1.
DR   TIGRFAMs; TIGR02937; sigma70-ECF; 1.
DR   PROSITE; PS00715; SIGMA70_1; 1.
DR   PROSITE; PS00716; SIGMA70_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; DNA-binding; Reference proteome; Sigma factor;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..239
FT                   /note="RNA polymerase sigma factor FliA"
FT                   /id="PRO_0000093981"
FT   DNA_BIND        207..226
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00962"
FT   REGION          16..88
FT                   /note="Sigma-70 factor domain-2"
FT   REGION          96..166
FT                   /note="Sigma-70 factor domain-3"
FT   REGION          185..233
FT                   /note="Sigma-70 factor domain-4"
FT   MOTIF           43..46
FT                   /note="Interaction with polymerase core subunit RpoC"
FT   MUTAGEN         73
FT                   /note="Q->A: No change in activity."
FT                   /evidence="ECO:0000269|PubMed:19400790"
FT   MUTAGEN         74
FT                   /note="R->A,W: Decrease in activity."
FT                   /evidence="ECO:0000269|PubMed:19400790"
FT   MUTAGEN         78
FT                   /note="A->E: Decrease in activity."
FT                   /evidence="ECO:0000269|PubMed:19400790"
FT   MUTAGEN         81
FT                   /note="D->A: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:19400790"
FT   MUTAGEN         84
FT                   /note="R->A: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:19400790"
FT   MUTAGEN         91
FT                   /note="R->A: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:19400790"
FT   MUTAGEN         92
FT                   /note="S->A: No change in activity."
FT                   /evidence="ECO:0000269|PubMed:19400790"
FT   MUTAGEN         94
FT                   /note="R->A: Decrease in activity."
FT                   /evidence="ECO:0000269|PubMed:19400790"
FT   MUTAGEN         95
FT                   /note="R->A: No change in activity."
FT                   /evidence="ECO:0000269|PubMed:19400790"
FT   MUTAGEN         96
FT                   /note="N->A: No change in activity."
FT                   /evidence="ECO:0000269|PubMed:19400790"
FT   MUTAGEN         98
FT                   /note="R->A: Strong decrease in activity."
FT                   /evidence="ECO:0000269|PubMed:19400790"
SQ   SEQUENCE   239 AA;  27521 MW;  B2930B44E1F24A33 CRC64;
     MNSLYTAEGV MDKHSLWQRY VPLVRHEALR LQVRLPASVE LDDLLQAGGI GLLNAVERYD
     ALQGTAFTTY AVQRIRGAML DELRSRDWVP RSVRRNAREV AQAIGQLEQE LGRNATETEV
     AERLGIDIAD YRQMLLDTNN SQLFSYDEWR EEHGDSIELV TDDHQRENPL QQLLDSNLRQ
     RVMEAIETLP EREKLVLTLY YQEELNLKEI GAVLEVGESR VSQLHSQAIK RLRTKLGKL
 
 
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