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P16575 (BVGS_BORPE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Virulence sensor protein BvgS

EC=2.7.13.3
Gene names
Name:bvgS
Ordered Locus Names:BP1877
OrganismBordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251) [Reference proteome] [HAMAP]
Taxonomic identifier257313 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella

Protein attributes

Sequence length1238 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Member of the two-component regulatory system BvgS/BvgA. Phosphorylates BvgA via a four-step phosphorelay in response to environmental signals.

Catalytic activity

ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.

Subcellular location

Cell inner membrane; Multi-pass membrane protein Probable.

Post-translational modification

Activation requires a sequential transfer of a phosphate group from a His in the primary transmitter domain, to an Asp in the receiver domain and to a His in the secondary transmitter domain.

Sequence similarities

Contains 1 histidine kinase domain.

Contains 1 HPt domain.

Contains 1 PAC (PAS-associated C-terminal) domain.

Contains 1 PAS (PER-ARNT-SIM) domain.

Contains 1 response regulatory domain.

Caution

Was originally (Ref.1) thought to be two separate ORFs named bvgB and bvgC.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3232 Potential
Chain33 – 12381206Virulence sensor protein BvgS
PRO_0000032370

Regions

Topological domain33 – 307275Cytoplasmic Potential
Transmembrane308 – 33124Helical; Potential
Topological domain332 – 541210Periplasmic Potential
Transmembrane542 – 56322Helical; Potential
Topological domain564 – 1238675Cytoplasmic Potential
Domain580 – 65172PAS
Domain652 – 70857PAC
Domain726 – 948223Histidine kinase
Domain974 – 1095122Response regulatory
Domain1133 – 122896HPt

Amino acid modifications

Modified residue7291Phosphohistidine; by autocatalysis Probable
Modified residue102314-aspartylphosphate Probable
Modified residue11721Phosphohistidine Probable

Experimental info

Mutagenesis7291H → Q: Loss of autophosphorylation. Ref.5
Mutagenesis9791D → G: Loss of activity; when associated with G-980. Ref.6
Mutagenesis9801D → G: Loss of activity. Ref.6
Mutagenesis10231D → G or N: Loss of activity. Ref.5 Ref.6
Mutagenesis10801K → L: Loss of activity. Ref.6
Mutagenesis1146 – 11472Missing: Loss of activity. Ref.6
Mutagenesis11721H → Q: Loss of activity. Ref.7
Sequence conflict7051K → E Ref.1
Sequence conflict7051K → E Ref.2
Sequence conflict10681R → A Ref.1
Sequence conflict10681R → A Ref.2

Secondary structure

............................................. 1238
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P16575 [UniParc].

Last modified September 19, 2003. Version 3.
Checksum: 28433439765ABC66

FASTA1,238135,001
        10         20         30         40         50         60 
MPAPHRLYPR SLICLAQALL AWALLAWAPA QASQELTLVG KAAVPDVEVA LDGDDWRWLA 

        70         80         90        100        110        120 
RKRVLTLGVY APDIPPFDVT YGERYEGLTA DYMAIIAHNL GMQAKVLRYP TREQALSALE 

       130        140        150        160        170        180 
SGQIDLIGTV NGTDGRQQSL RLSVPYAADH PVIVMPIGAR HVPASNLAGQ RLAVDINYLP 

       190        200        210        220        230        240 
KETLARAYPQ ATLHYFPSSE QALAAVAYGQ ADVFIGDALT TSHLVSQSYF NDVRVVAPAH 

       250        260        270        280        290        300 
IATGGESFGV RADNTRLLRV VNAVLEAIPP SEHRSLIYRW GLGSSISLDF AHPAYSAREQ 

       310        320        330        340        350        360 
QWMADHPVVK VAVLNLFAPF TLFRTDEQFG GISAAVLQLL QLRTGLDFEI IGVDTVEELI 

       370        380        390        400        410        420 
AKLRSGEADM AGALFVNSAR ESFLSFSRPY VRNGMVIVTR QDPDAPVDAD HLDGRTVALV 

       430        440        450        460        470        480 
RNSAAIPLLQ RRYPQAKVVT ADNPSEAMLM VANGQADAVV QTQISASYYV NRYFAGKLRI 

       490        500        510        520        530        540 
ASALDLPPAE IALATTRGQT ELMSILNKAL YSISNDELAS IISRWRGSDG DPRTWYAYRN 

       550        560        570        580        590        600 
EIYLLIGLGL LSALLFLSWI VYLRRQIRQR KRAERALNDQ LEFMRVLIDG TPNPIYVRDK 

       610        620        630        640        650        660 
EGRMLLCNDA YLDTFGVTAD AVLGKTIPEA NVVGDPALAR EMHEFLLTRV AAEREPRFED 

       670        680        690        700        710        720 
RDVTLHGRTR HVYQWTIPYG DSLGELKGII GGWIDITERA ELLRKLHDAK ESADAANRAK 

       730        740        750        760        770        780 
TTFLATMSHE IRTPMNAIIG MLELALLRPT DQEPDRQSIQ VAYDSARSLL ELIGDILDIA 

       790        800        810        820        830        840 
KIEAGKFDLA PVRTALRVLP EGAIRVFDGL ARQKGIELVL KTDIVGVDDV LIDPLRMKQV 

       850        860        870        880        890        900 
LSNLVGNAIK FTTEGQVVLA VTARPDGDAA HVQFSVSDTG CGISEADQRQ LFKPFSQVGG 

       910        920        930        940        950        960 
SAEAGPAPGT GLGLSISRRL VELMGGTLVM RSAPGVGTTV SVDLRLTMVE KSVQAAPPAA 

       970        980        990       1000       1010       1020 
ATAATPSKPQ VSLRVLVVDD HKPNLMLLRQ QLDYLGQRVI AADSGEAALA LWREHAFDVV 

      1030       1040       1050       1060       1070       1080 
ITDCNMPGIS GYELARRIRA AEAAPGYGRT RCILFGFTAS AQMDEAQRCR AAGMDDCLFK 

      1090       1100       1110       1120       1130       1140 
PIGVDALRQR LNEAVARAAL PTPPSPQAAA PATDDATPTA FSAESILALT QNDEALIRQL 

      1150       1160       1170       1180       1190       1200 
LEEVIRTNRA DVDQLQKLHQ QADWPKVSDM AHRLAGGARV VDAKAMIDTV LALEKKAQGQ 

      1210       1220       1230 
AGPSPEIDGL VRTLAAQSAA LETQLRAWLE QRPHQDQP 

« Hide

References

« Hide 'large scale' references
[1]"Sequences required for expression of Bordetella pertussis virulence factors share homology with prokaryotic signal transduction proteins."
Arico B., Miller J.F., Roy C., Stibitz S., Monack D.M., Falkow S., Gross R., Rappuoli R.
Proc. Natl. Acad. Sci. U.S.A. 86:6671-6675(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Structural and genetic analysis of the bvg locus in Bordetella species."
Arico B., Scarlato V., Monack D.M., Falkow S., Rappuoli R.
Mol. Microbiol. 5:2481-2491(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SEQUENCE REVISION.
[3]"Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica."
Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S. expand/collapse author list , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J.
Nat. Genet. 35:32-40(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Tohama I / ATCC BAA-589 / NCTC 13251.
[4]"Phase variation in Bordetella pertussis by frameshift mutation in a gene for a novel two-component system."
Stibitz S., Aaronson W., Monack D., Falkow S.
Nature 338:266-269(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 827-1153.
[5]"Autophosphorylation and phosphotransfer in the Bordetella pertussis BvgAS signal transduction cascade."
Uhl M.A., Miller J.F.
Proc. Natl. Acad. Sci. U.S.A. 91:1163-1167(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF HIS-729 AND ASP-1023.
[6]"In vivo characterization of the unorthodox BvgS two-component sensor protein of Bordetella pertussis."
Beier D., Schwarz B., Fuchs T.M., Gross R.
J. Mol. Biol. 248:596-610(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ASP-979; ASP-980; ASP-1023; LYS-1080; ARG-1146 AND THR-1147.
Strain: Tohama I / ATCC BAA-589 / NCTC 13251.
[7]"Integration of multiple domains in a two-component sensor protein: the Bordetella pertussis BvgAS phosphorelay."
Uhl M.A., Miller J.F.
EMBO J. 15:1028-1036(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, MUTAGENESIS OF HIS-1172.
[8]"Specificity of the BvgAS and EvgAS phosphorelay is mediated by the C-terminal HPt domains of the sensor proteins."
Perraud A.-L., Kimmel B., Weiss V., Gross R.
Mol. Microbiol. 27:875-887(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M25401 Genomic DNA. Translation: AAA22970.1.
BX640416 Genomic DNA. Translation: CAE42160.1.
PIRA40185.
RefSeqNP_880569.1. NC_002929.2.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3MPKX-ray2.04A287-542[»]
3MPLX-ray2.10A287-542[»]
ProteinModelPortalP16575.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING257313.BP1877.

Proteomic databases

PRIDEP16575.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE42160; CAE42160; BP1877.
GeneID2667057.
KEGGbpe:BP1877.
PATRIC21157042. VBIBorPer7866_2016.

Phylogenomic databases

eggNOGCOG0642.
HOGENOMHOG000269369.
KOK07679.
OMAAPAHIAT.
OrthoDBEOG6G4VQG.

Enzyme and pathway databases

BioCycBPER257313:BP1877-MONOMER.
BRENDA2.7.13.3. 899.

Family and domain databases

Gene3D1.10.287.130. 1 hit.
1.20.120.160. 1 hit.
3.30.565.10. 1 hit.
InterProIPR011006. CheY-like_superfamily.
IPR003661. EnvZ-like_dim/P.
IPR003594. HATPase_ATP-bd.
IPR000014. PAS.
IPR000700. PAS-assoc_C.
IPR013767. PAS_fold.
IPR001638. SBP_bac_3.
IPR004358. Sig_transdc_His_kin-like_C.
IPR008207. Sig_transdc_His_kin_Hpt_dom.
IPR005467. Sig_transdc_His_kinase_core.
IPR009082. Sig_transdc_His_kinase_dimeric.
IPR001789. Sig_transdc_resp-reg_receiver.
[Graphical view]
PfamPF02518. HATPase_c. 1 hit.
PF00512. HisKA. 1 hit.
PF01627. Hpt. 1 hit.
PF00989. PAS. 1 hit.
PF00072. Response_reg. 1 hit.
PF00497. SBP_bac_3. 2 hits.
[Graphical view]
PRINTSPR00344. BCTRLSENSOR.
SMARTSM00387. HATPase_c. 1 hit.
SM00388. HisKA. 1 hit.
SM00073. HPT. 1 hit.
SM00091. PAS. 1 hit.
SM00062. PBPb. 2 hits.
SM00448. REC. 1 hit.
[Graphical view]
SUPFAMSSF47226. SSF47226. 2 hits.
SSF47384. SSF47384. 1 hit.
SSF52172. SSF52172. 1 hit.
SSF55785. SSF55785. 1 hit.
SSF55874. SSF55874. 1 hit.
TIGRFAMsTIGR00229. sensory_box. 1 hit.
PROSITEPS50109. HIS_KIN. 1 hit.
PS50894. HPT. 1 hit.
PS50113. PAC. 1 hit.
PS50112. PAS. 1 hit.
PS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP16575.

Entry information

Entry nameBVGS_BORPE
AccessionPrimary (citable) accession number: P16575
Secondary accession number(s): P16576
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: September 19, 2003
Last modified: July 9, 2014
This is version 140 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references