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Protein

Transcriptional regulatory protein LiaR

Gene

liaR

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Member of the two-component regulatory system LiaS/LiaR probably involved in response to a subset of cell wall-active antibiotics that interfere with the lipid II cycle in the cytoplasmic membrane (bacitracin, nisin, ramoplanin and vancomycin). Seems also involved in response to cationic antimicrobial peptides and secretion stress. LiaR regulates the transcription of the liaIHGFSR operon.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi167 – 18620H-T-H motifPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation, Two-component regulatory system

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciBSUB:BSU33080-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcriptional regulatory protein LiaR
Gene namesi
Name:liaR
Synonyms:yvqC
Ordered Locus Names:BSU33080
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 211211Transcriptional regulatory protein LiaRPRO_0000081114Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei54 – 5414-aspartylphosphatePROSITE-ProRule annotation

Post-translational modificationi

Phosphorylated by LiaS.Curated

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO32197.

Expressioni

Inductioni

Autoregulated. Induced by antibiotics (vancomycin, bacitracin, nisin and ramoplanin), cationic antimicrobial peptides (human LL-37 and porcine PG-1), Triton X-100 and severe secretion stress.4 Publications

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100017956.

Structurei

3D structure databases

ProteinModelPortaliO32197.
SMRiO32197. Positions 1-210.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 119117Response regulatoryPROSITE-ProRule annotationAdd
BLAST
Domaini143 – 20866HTH luxR-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 HTH luxR-type DNA-binding domain.PROSITE-ProRule annotation
Contains 1 response regulatory domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105WH1. Bacteria.
COG2197. LUCA.
HOGENOMiHOG000034813.
InParanoidiO32197.
KOiK11618.
OMAiCIMLSVH.
OrthoDBiEOG69GZGV.
PhylomeDBiO32197.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR011006. CheY-like_superfamily.
IPR016032. Sig_transdc_resp-reg_C-effctor.
IPR001789. Sig_transdc_resp-reg_receiver.
IPR000792. Tscrpt_reg_LuxR_C.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00196. GerE. 1 hit.
PF00072. Response_reg. 1 hit.
[Graphical view]
PRINTSiPR00038. HTHLUXR.
SMARTiSM00421. HTH_LUXR. 1 hit.
SM00448. REC. 1 hit.
[Graphical view]
SUPFAMiSSF46894. SSF46894. 1 hit.
SSF52172. SSF52172. 1 hit.
PROSITEiPS00622. HTH_LUXR_1. 1 hit.
PS50043. HTH_LUXR_2. 1 hit.
PS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O32197-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIRVLLIDDH EMVRMGLAAF LEAQPDIEVI GEASDGSEGV RLAVELSPDV
60 70 80 90 100
ILMDLVMEGM DGIEATKQIC RELSDPKIIV LTSFIDDDKV YPVIEAGALS
110 120 130 140 150
YLLKTSKAAE IADAIRAASK GEPKLESKVA GKVLSRLRHS GENALPHESL
160 170 180 190 200
TKRELEILCL IAEGKTNKEI GEELFITIKT VKTHITNILS KLDVSDRTQA
210
AVYAHRNHLV N
Length:211
Mass (Da):23,125
Last modified:January 1, 1998 - v1
Checksum:iADBA4BAE61E3F5A8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ223978 Genomic DNA. Translation: CAA11745.1.
AL009126 Genomic DNA. Translation: CAB15298.1.
PIRiE70045.
RefSeqiNP_391188.1. NC_000964.3.
WP_003243201.1. NZ_JNCM01000033.1.

Genome annotation databases

EnsemblBacteriaiCAB15298; CAB15298; BSU33080.
GeneIDi935957.
KEGGibsu:BSU33080.
PATRICi18978604. VBIBacSub10457_3465.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ223978 Genomic DNA. Translation: CAA11745.1.
AL009126 Genomic DNA. Translation: CAB15298.1.
PIRiE70045.
RefSeqiNP_391188.1. NC_000964.3.
WP_003243201.1. NZ_JNCM01000033.1.

3D structure databases

ProteinModelPortaliO32197.
SMRiO32197. Positions 1-210.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100017956.

Proteomic databases

PaxDbiO32197.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15298; CAB15298; BSU33080.
GeneIDi935957.
KEGGibsu:BSU33080.
PATRICi18978604. VBIBacSub10457_3465.

Phylogenomic databases

eggNOGiENOG4105WH1. Bacteria.
COG2197. LUCA.
HOGENOMiHOG000034813.
InParanoidiO32197.
KOiK11618.
OMAiCIMLSVH.
OrthoDBiEOG69GZGV.
PhylomeDBiO32197.

Enzyme and pathway databases

BioCyciBSUB:BSU33080-MONOMER.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR011006. CheY-like_superfamily.
IPR016032. Sig_transdc_resp-reg_C-effctor.
IPR001789. Sig_transdc_resp-reg_receiver.
IPR000792. Tscrpt_reg_LuxR_C.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00196. GerE. 1 hit.
PF00072. Response_reg. 1 hit.
[Graphical view]
PRINTSiPR00038. HTHLUXR.
SMARTiSM00421. HTH_LUXR. 1 hit.
SM00448. REC. 1 hit.
[Graphical view]
SUPFAMiSSF46894. SSF46894. 1 hit.
SSF52172. SSF52172. 1 hit.
PROSITEiPS00622. HTH_LUXR_1. 1 hit.
PS50043. HTH_LUXR_2. 1 hit.
PS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The yvsA-yvqA (293 degrees - 289 degrees) region of the Bacillus subtilis chromosome containing genes involved in metal ion uptake and a putative sigma factor."
    Wipat A., Brignell C.S., Guy J.B., Rose M., Emmerson P.T., Harwood C.R.
    Microbiology 144:1593-1600(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  3. "Comprehensive DNA microarray analysis of Bacillus subtilis two-component regulatory systems."
    Kobayashi K., Ogura M., Yamaguchi H., Yoshida K., Ogasawara N., Tanaka T., Fujita Y.
    J. Bacteriol. 183:7365-7370(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  4. "Cell wall stress responses in Bacillus subtilis: the regulatory network of the bacitracin stimulon."
    Mascher T., Margulis N.G., Wang T., Ye R.W., Helmann J.D.
    Mol. Microbiol. 50:1591-1604(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY BACITRACIN.
    Strain: 168 / CU1065.
  5. "Antibiotic-inducible promoter regulated by the cell envelope stress-sensing two-component system LiaRS of Bacillus subtilis."
    Mascher T., Zimmer S.L., Smith T.-A., Helmann J.D.
    Antimicrob. Agents Chemother. 48:2888-2896(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION BY ANTIBIOTICS.
  6. "Transcriptome analysis of the secretion stress response of Bacillus subtilis."
    Hyyrylaeinen H.-L., Sarvas M., Kontinen V.P.
    Appl. Microbiol. Biotechnol. 67:389-396(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY STRESS.
  7. "Cationic antimicrobial peptides elicit a complex stress response in Bacillus subtilis that involves ECF-type sigma factors and two-component signal transduction systems."
    Pietiaeinen M., Gardemeister M., Mecklin M., Leskelae S., Sarvas M., Kontinen V.P.
    Microbiology 151:1577-1592(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY LL-37; PG-1 AND TRITON X-100.
    Strain: 168.

Entry informationi

Entry nameiLIAR_BACSU
AccessioniPrimary (citable) accession number: O32197
Secondary accession number(s): Q7B2J3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: January 1, 1998
Last modified: February 17, 2016
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.