RCSB_ECOLX
ID RCSB_ECOLX Reviewed; 216 AA.
AC P0DMC8; P14374; P69407;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 1.
DT 25-MAY-2022, entry version 54.
DE RecName: Full=Transcriptional regulatory protein RcsB {ECO:0000255|HAMAP-Rule:MF_00981};
GN Name=rcsB {ECO:0000255|HAMAP-Rule:MF_00981};
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN CAPSULAR POLYSACCHARIDE
RP SYNTHESIS.
RC STRAIN=O9:K30:H12;
RX PubMed=8366025; DOI=10.1128/jb.175.17.5384-5394.1993;
RA Jayaratne P., Keenleyside W.J., Maclachlan P.R., Dodgson C., Whitfield C.;
RT "Characterization of rcsB and rcsC from Escherichia coli O9:K30:H12 and
RT examination of the role of the rcs regulatory system in expression of group
RT I capsular polysaccharides.";
RL J. Bacteriol. 175:5384-5394(1993).
CC -!- FUNCTION: Component of the Rcs signaling system, which controls
CC transcription of numerous genes. RcsB is the response regulator that
CC binds to regulatory DNA regions. Can function both in an RcsA-dependent
CC or RcsA-independent manner (By similarity). Involved in regulation of
CC K30 capsular polysaccharide synthesis. {ECO:0000255|HAMAP-
CC Rule:MF_00981, ECO:0000269|PubMed:8366025}.
CC -!- SUBUNIT: Interacts with RcsD and RcsA. {ECO:0000255|HAMAP-
CC Rule:MF_00981}.
CC -!- PTM: Phosphorylated and activated by RcsD. {ECO:0000255|HAMAP-
CC Rule:MF_00981}.
CC -!- SIMILARITY: Belongs to the RcsB family. {ECO:0000255|HAMAP-
CC Rule:MF_00981}.
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DR EMBL; L11272; AAA24506.1; -; Genomic_DNA.
DR PIR; JV0068; BVECCB.
DR RefSeq; WP_001061917.1; NZ_WWEV01000106.1.
DR AlphaFoldDB; P0DMC8; -.
DR SMR; P0DMC8; -.
DR STRING; 585034.ECIAI1_2301; -.
DR GeneID; 67373623; -.
DR eggNOG; COG2197; Bacteria.
DR OMA; TITMIDN; -.
DR OrthoDB; 1687028at2; -.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-UniRule.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR CDD; cd06170; LuxR_C_like; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR HAMAP; MF_00981; RcsB; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR030864; RcsB.
DR InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR000792; Tscrpt_reg_LuxR_C.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF00196; GerE; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00038; HTHLUXR.
DR SMART; SM00421; HTH_LUXR; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF46894; SSF46894; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR PROSITE; PS00622; HTH_LUXR_1; 1.
DR PROSITE; PS50043; HTH_LUXR_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Phosphoprotein; Transcription; Transcription regulation;
KW Two-component regulatory system.
FT CHAIN 1..216
FT /note="Transcriptional regulatory protein RcsB"
FT /id="PRO_0000425416"
FT DOMAIN 5..124
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DOMAIN 144..209
FT /note="HTH luxR-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00981"
FT DNA_BIND 168..187
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00981"
FT MOD_RES 56
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00981"
SQ SEQUENCE 216 AA; 23671 MW; A78D1BD3004E0680 CRC64;
MNNMNVIIAD DHPIVLFGIR KSLEQIEWVN VVGEFEDSTA LINNLPKLDA HVLITDLSMP
GDKYGDGITL IKYIKRHFPS LSIIVLTMNN NPAILSAVLD LDIEGIVLKQ GAPTDLPKAL
AALQKGKKFT PESVSRLLEK ISAGGYGDKR LSPKESEVLR LFAEGFLVTE IAKKLNRSIK
TISSQKKSAM MKLGVENDIA LLNYLSSVTL SPADKD
