RCSA_ECOLI
ID RCSA_ECOLI Reviewed; 207 AA.
AC P0DMC9; P24210; P69405; Q47585;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 1.
DT 25-MAY-2022, entry version 42.
DE RecName: Full=Transcriptional regulatory protein RcsA {ECO:0000255|HAMAP-Rule:MF_00982};
DE AltName: Full=Colanic acid capsular biosynthesis activation protein A;
GN Name=rcsA {ECO:0000255|HAMAP-Rule:MF_00982};
GN OrderedLocusNames=b1951, JW1935;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-8, FUNCTION,
RP DEGRADATION BY LON PROTEASE, AND MUTAGENESIS OF MET-145.
RX PubMed=1999391; DOI=10.1128/jb.173.5.1738-1747.1991;
RA Stout V., Torres-Cabassa A., Maurizi M.R., Gutnick D., Gottesman S.;
RT "RcsA, an unstable positive regulator of capsular polysaccharide
RT synthesis.";
RL J. Bacteriol. 173:1738-1747(1991).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20, AND INDUCTION.
RC STRAIN=K12;
RX PubMed=7534408; DOI=10.1073/pnas.92.6.2003;
RA Sledjeski D., Gottesman S.;
RT "A small RNA acts as an antisilencer of the H-NS-silenced rcsA gene of
RT Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:2003-2007(1995).
RN [6]
RP FUNCTION, INTERACTION WITH RCSB, INDUCTION, AND BINDING TO RCSAB BOX.
RX PubMed=10702265; DOI=10.1074/jbc.275.10.7013;
RA Wehland M., Bernhard F.;
RT "The RcsAB box. Characterization of a new operator essential for the
RT regulation of exopolysaccharide biosynthesis in enteric bacteria.";
RL J. Biol. Chem. 275:7013-7020(2000).
RN [7]
RP DEGRADATION BY HSLUV PROTEASE.
RX PubMed=14766922; DOI=10.1099/mic.0.26446-0;
RA Kuo M.S., Chen K.P., Wu W.F.;
RT "Regulation of RcsA by the ClpYQ (HslUV) protease in Escherichia coli.";
RL Microbiology 150:437-446(2004).
CC -!- FUNCTION: Component of the Rcs signaling system, which controls
CC transcription of numerous genes. Binds, with RcsB, to the RcsAB box to
CC regulate expression of genes involved in colanic acid capsule
CC synthesis. {ECO:0000255|HAMAP-Rule:MF_00982,
CC ECO:0000269|PubMed:10702265, ECO:0000269|PubMed:1999391}.
CC -!- SUBUNIT: Interacts with RcsB. {ECO:0000255|HAMAP-Rule:MF_00982,
CC ECO:0000269|PubMed:10702265}.
CC -!- INDUCTION: Autoregulated. Repressed by H-NS. Induced by the DsrA small
CC regulatory RNA, which inhibits the H-NS mediated transcriptional
CC silencing. {ECO:0000269|PubMed:10702265, ECO:0000269|PubMed:7534408}.
CC -!- PTM: Degraded by the Lon and the HslUV proteases (PubMed:1999391 and
CC PubMed:14766922). Interaction with RcsB protects RcsA from degradation
CC (PubMed:1999391). {ECO:0000269|PubMed:1999391}.
CC -!- SIMILARITY: Belongs to the RcsA family. {ECO:0000255|HAMAP-
CC Rule:MF_00982}.
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DR EMBL; M58003; AAA82970.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75018.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15776.1; -; Genomic_DNA.
DR EMBL; U17137; AAC43315.1; -; Genomic_DNA.
DR PIR; A37320; A37320.
DR RefSeq; NP_416461.1; NC_000913.3.
DR RefSeq; WP_000104001.1; NZ_LN832404.1.
DR AlphaFoldDB; P0DMC9; -.
DR SMR; P0DMC9; -.
DR BioGRID; 4261047; 8.
DR ComplexPortal; CPX-5762; rcsAB DNA-binding transcription factor complex.
DR IntAct; P0DMC9; 29.
DR STRING; 511145.b1951; -.
DR PaxDb; P0DMC9; -.
DR PRIDE; P0DMC9; -.
DR EnsemblBacteria; AAC75018; AAC75018; b1951.
DR EnsemblBacteria; BAA15776; BAA15776; BAA15776.
DR GeneID; 946467; -.
DR KEGG; ecj:JW1935; -.
DR KEGG; eco:b1951; -.
DR PATRIC; fig|1411691.4.peg.300; -.
DR EchoBASE; EB0813; -.
DR eggNOG; COG2197; Bacteria.
DR HOGENOM; CLU_105065_0_0_6; -.
DR OMA; ANIHFDE; -.
DR PhylomeDB; P0DMC9; -.
DR BioCyc; EcoCyc:PD02233; -.
DR PRO; PR:P0DMC9; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005667; C:transcription regulator complex; IPI:ComplexPortal.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:ComplexPortal.
DR GO; GO:1902021; P:regulation of bacterial-type flagellum-dependent cell motility; IC:ComplexPortal.
DR GO; GO:1901913; P:regulation of capsule organization; IDA:ComplexPortal.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IDA:EcoCyc.
DR CDD; cd06170; LuxR_C_like; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR HAMAP; MF_00982; RcsA; 1.
DR InterPro; IPR030866; RcsA.
DR InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
DR InterPro; IPR000792; Tscrpt_reg_LuxR_C.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF00196; GerE; 1.
DR PRINTS; PR00038; HTHLUXR.
DR SMART; SM00421; HTH_LUXR; 1.
DR SUPFAM; SSF46894; SSF46894; 1.
DR PROSITE; PS00622; HTH_LUXR_1; 1.
DR PROSITE; PS50043; HTH_LUXR_2; 1.
PE 1: Evidence at protein level;
KW Activator; Capsule biogenesis/degradation; Direct protein sequencing;
KW DNA-binding; Reference proteome; Sensory transduction; Transcription;
KW Transcription regulation.
FT CHAIN 1..207
FT /note="Transcriptional regulatory protein RcsA"
FT /id="PRO_0000184178"
FT DOMAIN 131..196
FT /note="HTH luxR-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00982"
FT DNA_BIND 155..174
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00982"
FT MUTAGEN 145
FT /note="M->V: In rcsA*; increases stability and capsule
FT synthesis."
FT /evidence="ECO:0000269|PubMed:1999391"
SQ SEQUENCE 207 AA; 23516 MW; 6DAA22097807AF62 CRC64;
MSTIIMDLCS YTRLGLTGYL LSRGVKKREI NDIETVDDLA IACDSQRPSV VFINEDCFIH
DASNSQRIKL IINQHPNTLF IVFMAIANVH FDEYLLVRKN LLISSKSIKP ESLDDILGDI
LKKETTITSF LNMPTLSLSR TESSMLRMWM AGQGTIQISD QMNIKAKTVS SHKGNIKRKI
KTHNKQVIYH VVRLTDNVTN GIFVNMR
