ID RCSB_SALTY Reviewed; 216 AA.
AC P58663;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2002, sequence version 1.
DT 01-MAY-2013, entry version 80.
DE RecName: Full=Capsular synthesis regulator component B;
GN Name=rcsB; OrderedLocusNames=STM2270;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M.,
RA Waterston R., Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium
RT LT2.";
RL Nature 413:852-856(2001).
CC -!- FUNCTION: RcsB is a member of the two-component regulatory system
CC RcsB/RcsC, which regulates the expression of genes involved in
CC colanic acid capsule synthesis. The two-component system interacts
CC with a phosphotransfer intermediate, YojN, which receives a
CC phosphoryl group from RcsC and transfers it to RscB. RcsB acts as
CC the effector. Additional control is provided by the dependence on
CC the alternate sigma factor, RpoN, for the synthesis of RcsB. RcsA
CC and RcsB form a complex to promote transcription of the genes for
CC capsule synthesis (By similarity).
CC -!- FUNCTION: Also stimulates ftsZ expression. This suggests that RcsB
CC is a regulator implicated in the regulation of more than one
CC cellular function (By similarity).
CC -!- PTM: Phosphorylation of the RcsB protein has not been
CC demonstrated, but RcsB has the potential of being phosphorylated
CC by a phosphotransfer intermediate molecule (YojN), and is more
CC active in its phosphorylated form (By similarity).
CC -!- SIMILARITY: Contains 1 HTH luxR-type DNA-binding domain.
CC -!- SIMILARITY: Contains 1 response regulatory domain.
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DR EMBL; AE006468; AAL21171.1; -; Genomic_DNA.
DR RefSeq; NP_461212.1; NC_003197.1.
DR ProteinModelPortal; P58663; -.
DR SMR; P58663; 129-215.
DR STRING; 99287.STM2270; -.
DR PaxDb; P58663; -.
DR PRIDE; P58663; -.
DR EnsemblBacteria; AAL21171; AAL21171; STM2270.
DR GeneID; 1253792; -.
DR KEGG; stm:STM2270; -.
DR PATRIC; 32383147; VBISalEnt20916_2403.
DR eggNOG; COG2197; -.
DR HOGENOM; HOG000034813; -.
DR KO; K07687; -.
DR OMA; MKLGVDN; -.
DR ProtClustDB; PRK10840; -.
DR GO; GO:0005622; C:intracellular; IEA:InterPro.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:GOC.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR011991; WHTH_DNA-bd_dom.
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; Bipartite_resp_reg_C-effector; 1.
DR SUPFAM; SSF52172; CheY_like; 1.
DR PROSITE; PS00622; HTH_LUXR_1; 1.
DR PROSITE; PS50043; HTH_LUXR_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
KW Activator; Capsule biogenesis/degradation; Complete proteome;
KW DNA-binding; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Two-component regulatory system.
FT CHAIN 1 216 Capsular synthesis regulator component B.
FT /FTId=PRO_0000081213.
FT DOMAIN 1 124 Response regulatory.
FT DOMAIN 144 209 HTH luxR-type.
FT DNA_BIND 168 187 H-T-H motif (By similarity).
FT MOD_RES 56 56 4-aspartylphosphate (By similarity).
SQ SEQUENCE 216 AA; 23715 MW; A63D1BCF704E0680 CRC64;
MNNMNVIIAD DHPIVLFGIR KSLEQIEWVN VVGEFEDSTA LINNLPKLDA HVLITDLSMP
GDKYGDGITL IKYIKRHFPS LSIIVLTMNN NPAILSAVLD LDIEGIVLKQ GAPTDLPKAL
AALQKGKKFT PESVSRLLEK ISAGGYGDKR LSPKESEVLR LFAEGFLVTE IAKKLNRSIK
TISSQKKSAM MKLGVENDIA LLNYLSSVTL SPTDKE
//
