Transcriptional regulatory protein BasR - Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)

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P36556 (BASR_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 96. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Transcriptional regulatory protein BasR

Gene names

Name:	basR
Synonyms:	parA, pmrA
Ordered Locus Names:	STM4292

Organism

Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]

Taxonomic identifier

99287 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella ›

Protein attributes

Sequence length	222 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Member of the two-component regulatory system BasS/BasR. BasR induces the transcription of the ugd, ais, arnBCADTEF and eptA-basRS loci, all involved in resistance to polymyxin. Represses the transcription of pmrD. Plays a role in the adaptation of the organism to the host environment, in particular to neutrophils, and therefore it plays a role in virulence as well. Ref.5 Ref.7
Subunit structure	Homodimer. Ref.5
Subcellular location	Cytoplasm Potential.
Induction	The eptA-basRS operon is positively autoregulated by BasR under high iron or aluminum concentration conditions. Ref.2 Ref.4 Ref.5 Ref.7
Post-translational modification	Phosphorylated by BasS. Ref.5 Ref.6
Miscellaneous	The activity of the BasR protein is controlled at a post-transcriptional level by the PmrD protein, under low Mg²⁺ concentration conditions.
Sequence similarities	Contains 1 response regulatory domain.

Ontologies

Keywords
Biological process	Antibiotic resistance Transcription Transcription regulation Two-component regulatory system Virulence
Cellular component	Cytoplasm
Ligand	DNA-binding
Molecular function	Activator Repressor
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	intracellular signal transduction Inferred from electronic annotation. Source: GOC pathogenesis Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW response to antibiotic Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW phosphorelay response regulator activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 222

222

Transcriptional regulatory protein BasR

PRO_0000081024

Regions

Domain

1 – 116

116

Response regulatory

Amino acid modifications

Modified residue

4-aspartylphosphate

Natural variations

Natural variant

H → R in strain: LT2 / SGSC1412 and S4194; resistance to polymyxin B and neutrophil proteins.

Experimental info

Mutagenesis

D → A: No activation of BasR regulated genes. Ref.6

Sequences

Sequence

Length

Mass (Da)

Tools

P36556 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 3734CC2034070533
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FASTA

222

25,035

        10         20         30         40         50         60 
MKILIVEDDT LLLQGLILAA QTEGYACDGV STARAAEHSL ESGHYSLMVL DLGLPDEDGL 

        70         80         90        100        110        120 
HFLTRIRQKK YTLPVLILTA HDTLNDRITG LDVGADDYLV KPFALEELHA RIRALLRRHN 

       130        140        150        160        170        180 
NQGESELTVG NLTLNIGRHQ AWRDGQELTL TPKEYALLSR LMLKAGSPVH REILYNDIYN 

       190        200        210        220 
WDNEPSTNTL EVHIHNLRDK VGKSRIRTVR GFGYMLVATE ES

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Spontaneous pmrA mutants of Salmonella typhimurium LT2 define a new two-component regulatory system with a possible role in virulence." Roland K.L., Martin L.E., Esther C.R., Spitznagel J.K. J. Bacteriol. 175:4154-4164(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: LT2.
[2]	"Phenotypic differences between Salmonella and Escherichia coli resulting from the disparate regulation of homologous genes." Winfield M.D., Groisman E.A. Proc. Natl. Acad. Sci. U.S.A. 101:17162-17167(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], REGULATION BY PMRD. Strain: S4194.
[3]	"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2." McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. Wilson R.K. Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: LT2 / SGSC1412 / ATCC 700720.
[4]	"PhoP-PhoQ activates transcription of pmrAB, encoding a two-component regulatory system involved in Salmonella typhimurium antimicrobial peptide resistance." Gunn J.S., Miller S.I. J. Bacteriol. 178:6857-6864(1996) [PubMed] [Europe PMC] [Abstract] Cited for: REGULATION. Strain: ATCC 14028s / SGSG 2262.
[5]	"Molecular characterization of the PmrA regulon." Woesten M.M.S.M., Groisman E.A. J. Biol. Chem. 274:27185-27190(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INDUCTION, PHOSPHORYLATION, SUBUNIT. Strain: ATCC 14028s / SGSG 2262.
[6]	"A small protein that mediates the activation of a two-component system by another two-component system." Kox L.F.F., Woesten M.M.S.M., Groisman E.A. EMBO J. 19:1861-1872(2000) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF ASP-51, PHOSPHORYLATION AT ASP-51. Strain: ATCC 14028s / SGSG 2262.
[7]	"Closing the loop: the PmrA/PmrB two-component system negatively controls expression of its posttranscriptional activator PmrD." Kato A., Latifi T., Groisman E.A. Proc. Natl. Acad. Sci. U.S.A. 100:4706-4711(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, REGULATION BY PMRD. Strain: ATCC 14028s / SGSG 2262.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L13395 Genomic DNA. Translation: AAA72365.1. AY725348 Genomic DNA. Translation: AAV92795.1. AE006468 Genomic DNA. Translation: AAL23116.1.
PIR	B40656.
RefSeq	NP_463157.1. NC_003197.1.
3D structure databases
ProteinModelPortal	P36556.
ModBase	Search...
Protein-protein interaction databases
STRING	99287.STM4292.
Proteomic databases
PaxDb	P36556.
PRIDE	P36556.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAL23116; AAL23116; STM4292.
GeneID	1255818.
KEGG	stm:STM4292.
PATRIC	32387493. VBISalEnt20916_4514.
Phylogenomic databases
eggNOG	COG0745.
HOGENOM	HOG000034815.
KO	K07771.
OMA	GKATIRT.
ProtClustDB	PRK10643.
Family and domain databases
Gene3D	1.10.10.10. 1 hit.
InterPro	IPR011006. CheY-like_superfamily. IPR001867. Sig_transdc_resp-reg_C. IPR001789. Sig_transdc_resp-reg_receiver. IPR011991. WHTH_DNA-bd_dom. [Graphical view]
Pfam	PF00072. Response_reg. 1 hit. PF00486. Trans_reg_C. 1 hit. [Graphical view]
SMART	SM00448. REC. 1 hit. SM00862. Trans_reg_C. 1 hit. [Graphical view]
SUPFAM	SSF52172. CheY_like. 1 hit.
PROSITE	PS50110. RESPONSE_REGULATORY. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

BASR_SALTY

Accession

Primary (citable) accession number: P36556
Secondary accession number(s): Q5MN92

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	May 1, 2013
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents