BASR_SALTY
ID BASR_SALTY Reviewed; 222 AA.
AC P36556; Q5MN92;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Transcriptional regulatory protein BasR;
GN Name=basR; Synonyms=parA, pmrA; OrderedLocusNames=STM4292;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=8391535; DOI=10.1128/jb.175.13.4154-4164.1993;
RA Roland K.L., Martin L.E., Esther C.R., Spitznagel J.K.;
RT "Spontaneous pmrA mutants of Salmonella typhimurium LT2 define a new two-
RT component regulatory system with a possible role in virulence.";
RL J. Bacteriol. 175:4154-4164(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND REGULATION BY PMRD.
RC STRAIN=S4194;
RX PubMed=15569938; DOI=10.1073/pnas.0406038101;
RA Winfield M.D., Groisman E.A.;
RT "Phenotypic differences between Salmonella and Escherichia coli resulting
RT from the disparate regulation of homologous genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:17162-17167(2004).
RN [3]
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., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [4]
RP REGULATION.
RC STRAIN=ATCC 14028s / SGSG 2262;
RX PubMed=8955307; DOI=10.1128/jb.178.23.6857-6864.1996;
RA Gunn J.S., Miller S.I.;
RT "PhoP-PhoQ activates transcription of pmrAB, encoding a two-component
RT regulatory system involved in Salmonella typhimurium antimicrobial peptide
RT resistance.";
RL J. Bacteriol. 178:6857-6864(1996).
RN [5]
RP FUNCTION, INDUCTION, PHOSPHORYLATION, AND SUBUNIT.
RC STRAIN=ATCC 14028s / SGSG 2262;
RX PubMed=10480935; DOI=10.1074/jbc.274.38.27185;
RA Woesten M.M.S.M., Groisman E.A.;
RT "Molecular characterization of the PmrA regulon.";
RL J. Biol. Chem. 274:27185-27190(1999).
RN [6]
RP MUTAGENESIS OF ASP-51, AND PHOSPHORYLATION AT ASP-51.
RC STRAIN=ATCC 14028s / SGSG 2262;
RX PubMed=10775270; DOI=10.1093/emboj/19.8.1861;
RA Kox L.F.F., Woesten M.M.S.M., Groisman E.A.;
RT "A small protein that mediates the activation of a two-component system by
RT another two-component system.";
RL EMBO J. 19:1861-1872(2000).
RN [7]
RP FUNCTION, AND REGULATION BY PMRD.
RC STRAIN=ATCC 14028s / SGSG 2262;
RX PubMed=12676988; DOI=10.1073/pnas.0836837100;
RA Kato A., Latifi T., Groisman E.A.;
RT "Closing the loop: the PmrA/PmrB two-component system negatively controls
RT expression of its posttranscriptional activator PmrD.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:4706-4711(2003).
CC -!- FUNCTION: Member of the two-component regulatory system BasS/BasR. BasR
CC induces the transcription of the ugd, ais, arnBCADTEF and eptA-basRS
CC loci, all involved in resistance to polymyxin. Represses the
CC transcription of pmrD. Plays a role in the adaptation of the organism
CC to the host environment, in particular to neutrophils, and therefore it
CC plays a role in virulence as well. {ECO:0000269|PubMed:10480935,
CC ECO:0000269|PubMed:12676988}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10480935}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: The eptA-basRS operon is positively autoregulated by BasR
CC under high iron or aluminum concentration conditions.
CC {ECO:0000269|PubMed:10480935}.
CC -!- PTM: Phosphorylated by BasS. {ECO:0000269|PubMed:10480935,
CC ECO:0000269|PubMed:10775270}.
CC -!- MISCELLANEOUS: The activity of the BasR protein is controlled at a
CC post-transcriptional level by the PmrD protein, under low Mg(2+)
CC concentration conditions.
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DR EMBL; L13395; AAA72365.1; -; Genomic_DNA.
DR EMBL; AY725348; AAV92795.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL23116.1; -; Genomic_DNA.
DR PIR; B40656; B40656.
DR RefSeq; NP_463157.1; NC_003197.2.
DR AlphaFoldDB; P36556; -.
DR SMR; P36556; -.
DR STRING; 99287.STM4292; -.
DR PaxDb; P36556; -.
DR EnsemblBacteria; AAL23116; AAL23116; STM4292.
DR GeneID; 1255818; -.
DR KEGG; stm:STM4292; -.
DR PATRIC; fig|99287.12.peg.4514; -.
DR HOGENOM; CLU_000445_30_1_6; -.
DR PhylomeDB; P36556; -.
DR BioCyc; SENT99287:STM4292-MON; -.
DR PHI-base; PHI:4497; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0032993; C:protein-DNA complex; IBA:GO_Central.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; IBA:GO_Central.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR CDD; cd00383; trans_reg_C; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR001867; OmpR/PhoB-type_DNA-bd.
DR InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR039420; WalR-like.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR48111; PTHR48111; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF00486; Trans_reg_C; 1.
DR SMART; SM00448; REC; 1.
DR SMART; SM00862; Trans_reg_C; 1.
DR SUPFAM; SSF46894; SSF46894; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR PROSITE; PS51755; OMPR_PHOB; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW Activator; Antibiotic resistance; Cytoplasm; DNA-binding; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Two-component regulatory system; Virulence.
FT CHAIN 1..222
FT /note="Transcriptional regulatory protein BasR"
FT /id="PRO_0000081024"
FT DOMAIN 2..116
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DNA_BIND 124..218
FT /note="OmpR/PhoB-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01091"
FT MOD_RES 51
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169,
FT ECO:0000269|PubMed:10775270"
FT VARIANT 81
FT /note="H -> R (in strain: LT2 / SGSC1412 and S4194;
FT resistance to polymyxin B and neutrophil proteins)"
FT MUTAGEN 51
FT /note="D->A: No activation of BasR regulated genes."
FT /evidence="ECO:0000269|PubMed:10775270"
SQ SEQUENCE 222 AA; 25035 MW; 3734CC2034070533 CRC64;
MKILIVEDDT LLLQGLILAA QTEGYACDGV STARAAEHSL ESGHYSLMVL DLGLPDEDGL
HFLTRIRQKK YTLPVLILTA HDTLNDRITG LDVGADDYLV KPFALEELHA RIRALLRRHN
NQGESELTVG NLTLNIGRHQ AWRDGQELTL TPKEYALLSR LMLKAGSPVH REILYNDIYN
WDNEPSTNTL EVHIHNLRDK VGKSRIRTVR GFGYMLVATE ES
