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Protein

Virulence sensor protein BvgS

Gene

bvgS

Organism
Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Two-component regulatory system, Virulence

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciBPER257313:BP1877-MONOMER.
BRENDAi2.7.13.3. 899.

Names & Taxonomyi

Protein namesi
Recommended name:
Virulence sensor protein BvgS (EC:2.7.13.3)
Gene namesi
Name:bvgS
Ordered Locus Names:BP1877
OrganismiBordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
Taxonomic identifieri257313 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella
ProteomesiUP000002676 Componenti: Chromosome

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini33 – 307275CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei308 – 33124HelicalSequence AnalysisAdd
BLAST
Topological domaini332 – 541210PeriplasmicSequence AnalysisAdd
BLAST
Transmembranei542 – 56322HelicalSequence AnalysisAdd
BLAST
Topological domaini564 – 1238675CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi729 – 7291H → Q: Loss of autophosphorylation. 1 Publication
Mutagenesisi979 – 9791D → G: Loss of activity; when associated with G-980. 1 Publication
Mutagenesisi980 – 9801D → G: Loss of activity. 1 Publication
Mutagenesisi1023 – 10231D → G or N: Loss of activity. 2 Publications
Mutagenesisi1080 – 10801K → L: Loss of activity. 1 Publication
Mutagenesisi1146 – 11472Missing : Loss of activity.
Mutagenesisi1172 – 11721H → Q: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3232Sequence AnalysisAdd
BLAST
Chaini33 – 12381206Virulence sensor protein BvgSPRO_0000032370Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei729 – 7291Phosphohistidine; by autocatalysisCurated
Modified residuei1023 – 102314-aspartylphosphateCurated
Modified residuei1172 – 11721PhosphohistidineCurated

Post-translational modificationi

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.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP16575.

Interactioni

Protein-protein interaction databases

STRINGi257313.BP1877.

Structurei

Secondary structure

1
1238
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi34 – 385Combined sources
Helixi54 – 629Combined sources
Beta strandi64 – 707Combined sources
Turni75 – 773Combined sources
Beta strandi79 – 813Combined sources
Beta strandi84 – 874Combined sources
Helixi88 – 9912Combined sources
Beta strandi103 – 1119Combined sources
Helixi112 – 1209Combined sources
Beta strandi125 – 1306Combined sources
Beta strandi134 – 1374Combined sources
Beta strandi139 – 1424Combined sources
Beta strandi151 – 1566Combined sources
Helixi164 – 1674Combined sources
Beta strandi170 – 1756Combined sources
Turni176 – 1783Combined sources
Helixi181 – 1877Combined sources
Beta strandi191 – 1988Combined sources
Helixi199 – 2079Combined sources
Beta strandi212 – 2176Combined sources
Helixi218 – 22811Combined sources
Turni229 – 2324Combined sources
Beta strandi233 – 2386Combined sources
Beta strandi246 – 2516Combined sources
Helixi255 – 26713Combined sources
Helixi270 – 27910Combined sources
Helixi283 – 2853Combined sources
Turni286 – 2883Combined sources
Helixi297 – 3059Combined sources
Beta strandi307 – 3148Combined sources
Turni318 – 3203Combined sources
Beta strandi321 – 3233Combined sources
Beta strandi329 – 3313Combined sources
Helixi332 – 34413Combined sources
Beta strandi347 – 3559Combined sources
Helixi356 – 36510Combined sources
Beta strandi369 – 3757Combined sources
Helixi378 – 3803Combined sources
Turni381 – 3833Combined sources
Beta strandi384 – 3863Combined sources
Beta strandi390 – 3934Combined sources
Beta strandi395 – 4028Combined sources
Helixi409 – 4113Combined sources
Beta strandi416 – 4205Combined sources
Helixi425 – 4328Combined sources
Beta strandi436 – 4438Combined sources
Helixi444 – 4529Combined sources
Beta strandi457 – 4626Combined sources
Helixi463 – 47311Combined sources
Turni475 – 4773Combined sources
Beta strandi478 – 4836Combined sources
Beta strandi489 – 4968Combined sources
Helixi500 – 51112Combined sources
Helixi515 – 5239Combined sources
Helixi532 – 54413Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3MPKX-ray2.04A287-542[»]
3MPLX-ray2.10A287-542[»]
4Q0CX-ray3.10A/B/C/D30-544[»]
ProteinModelPortaliP16575.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16575.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini580 – 65172PASPROSITE-ProRule annotationAdd
BLAST
Domaini652 – 70857PACPROSITE-ProRule annotationAdd
BLAST
Domaini726 – 948223Histidine kinasePROSITE-ProRule annotationAdd
BLAST
Domaini974 – 1095122Response regulatoryPROSITE-ProRule annotationAdd
BLAST
Domaini1133 – 122896HPtPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 histidine kinase domain.PROSITE-ProRule annotation
Contains 1 HPt domain.PROSITE-ProRule annotation
Contains 1 PAC (PAS-associated C-terminal) domain.PROSITE-ProRule annotation
Contains 1 PAS (PER-ARNT-SIM) domain.PROSITE-ProRule annotation
Contains 1 response regulatory domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0642.
HOGENOMiHOG000269369.
KOiK07679.
OMAiFMRVLID.
OrthoDBiEOG6G4VQG.

Family and domain databases

Gene3Di1.10.287.130. 1 hit.
1.20.120.160. 1 hit.
3.30.565.10. 1 hit.
InterProiIPR011006. CheY-like_superfamily.
IPR003661. EnvZ-like_dim/P.
IPR003594. HATPase_C.
IPR000014. PAS.
IPR000700. PAS-assoc_C.
IPR013767. PAS_fold.
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.
IPR001638. Solute-binding_3/MltF_N.
[Graphical view]
PfamiPF02518. HATPase_c. 1 hit.
PF00512. HisKA. 1 hit.
PF01627. Hpt. 1 hit.
PF00989. PAS. 1 hit.
PF00072. Response_reg. 1 hit.
[Graphical view]
PRINTSiPR00344. BCTRLSENSOR.
SMARTiSM00387. 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]
SUPFAMiSSF47226. SSF47226. 2 hits.
SSF47384. SSF47384. 1 hit.
SSF52172. SSF52172. 1 hit.
SSF55785. SSF55785. 1 hit.
SSF55874. SSF55874. 1 hit.
TIGRFAMsiTIGR00229. sensory_box. 1 hit.
PROSITEiPS50109. HIS_KIN. 1 hit.
PS50894. HPT. 1 hit.
PS50113. PAC. 1 hit.
PS50112. PAS. 1 hit.
PS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P16575-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPAPHRLYPR SLICLAQALL AWALLAWAPA QASQELTLVG KAAVPDVEVA
60 70 80 90 100
LDGDDWRWLA RKRVLTLGVY APDIPPFDVT YGERYEGLTA DYMAIIAHNL
110 120 130 140 150
GMQAKVLRYP TREQALSALE SGQIDLIGTV NGTDGRQQSL RLSVPYAADH
160 170 180 190 200
PVIVMPIGAR HVPASNLAGQ RLAVDINYLP KETLARAYPQ ATLHYFPSSE
210 220 230 240 250
QALAAVAYGQ ADVFIGDALT TSHLVSQSYF NDVRVVAPAH IATGGESFGV
260 270 280 290 300
RADNTRLLRV VNAVLEAIPP SEHRSLIYRW GLGSSISLDF AHPAYSAREQ
310 320 330 340 350
QWMADHPVVK VAVLNLFAPF TLFRTDEQFG GISAAVLQLL QLRTGLDFEI
360 370 380 390 400
IGVDTVEELI AKLRSGEADM AGALFVNSAR ESFLSFSRPY VRNGMVIVTR
410 420 430 440 450
QDPDAPVDAD HLDGRTVALV RNSAAIPLLQ RRYPQAKVVT ADNPSEAMLM
460 470 480 490 500
VANGQADAVV QTQISASYYV NRYFAGKLRI ASALDLPPAE IALATTRGQT
510 520 530 540 550
ELMSILNKAL YSISNDELAS IISRWRGSDG DPRTWYAYRN EIYLLIGLGL
560 570 580 590 600
LSALLFLSWI VYLRRQIRQR KRAERALNDQ LEFMRVLIDG TPNPIYVRDK
610 620 630 640 650
EGRMLLCNDA YLDTFGVTAD AVLGKTIPEA NVVGDPALAR EMHEFLLTRV
660 670 680 690 700
AAEREPRFED RDVTLHGRTR HVYQWTIPYG DSLGELKGII GGWIDITERA
710 720 730 740 750
ELLRKLHDAK ESADAANRAK TTFLATMSHE IRTPMNAIIG MLELALLRPT
760 770 780 790 800
DQEPDRQSIQ VAYDSARSLL ELIGDILDIA KIEAGKFDLA PVRTALRVLP
810 820 830 840 850
EGAIRVFDGL ARQKGIELVL KTDIVGVDDV LIDPLRMKQV LSNLVGNAIK
860 870 880 890 900
FTTEGQVVLA VTARPDGDAA HVQFSVSDTG CGISEADQRQ LFKPFSQVGG
910 920 930 940 950
SAEAGPAPGT GLGLSISRRL VELMGGTLVM RSAPGVGTTV SVDLRLTMVE
960 970 980 990 1000
KSVQAAPPAA ATAATPSKPQ VSLRVLVVDD HKPNLMLLRQ QLDYLGQRVI
1010 1020 1030 1040 1050
AADSGEAALA LWREHAFDVV ITDCNMPGIS GYELARRIRA AEAAPGYGRT
1060 1070 1080 1090 1100
RCILFGFTAS AQMDEAQRCR AAGMDDCLFK PIGVDALRQR LNEAVARAAL
1110 1120 1130 1140 1150
PTPPSPQAAA PATDDATPTA FSAESILALT QNDEALIRQL LEEVIRTNRA
1160 1170 1180 1190 1200
DVDQLQKLHQ QADWPKVSDM AHRLAGGARV VDAKAMIDTV LALEKKAQGQ
1210 1220 1230
AGPSPEIDGL VRTLAAQSAA LETQLRAWLE QRPHQDQP
Length:1,238
Mass (Da):135,001
Last modified:September 19, 2003 - v3
Checksum:i28433439765ABC66
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti705 – 7051K → E (PubMed:2549542).Curated
Sequence conflicti705 – 7051K → E (PubMed:1791760).Curated
Sequence conflicti1068 – 10681R → A (PubMed:2549542).Curated
Sequence conflicti1068 – 10681R → A (PubMed:1791760).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M25401 Genomic DNA. Translation: AAA22970.1.
BX640416 Genomic DNA. Translation: CAE42160.1.
PIRiA40185.
RefSeqiNP_880569.1. NC_002929.2.
WP_010930608.1. NC_002929.2.

Genome annotation databases

EnsemblBacteriaiCAE42160; CAE42160; BP1877.
GeneIDi2667057.
KEGGibpe:BP1877.
PATRICi21157042. VBIBorPer7866_2016.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M25401 Genomic DNA. Translation: AAA22970.1.
BX640416 Genomic DNA. Translation: CAE42160.1.
PIRiA40185.
RefSeqiNP_880569.1. NC_002929.2.
WP_010930608.1. NC_002929.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3MPKX-ray2.04A287-542[»]
3MPLX-ray2.10A287-542[»]
4Q0CX-ray3.10A/B/C/D30-544[»]
ProteinModelPortaliP16575.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi257313.BP1877.

Proteomic databases

PRIDEiP16575.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAE42160; CAE42160; BP1877.
GeneIDi2667057.
KEGGibpe:BP1877.
PATRICi21157042. VBIBorPer7866_2016.

Phylogenomic databases

eggNOGiCOG0642.
HOGENOMiHOG000269369.
KOiK07679.
OMAiFMRVLID.
OrthoDBiEOG6G4VQG.

Enzyme and pathway databases

BioCyciBPER257313:BP1877-MONOMER.
BRENDAi2.7.13.3. 899.

Miscellaneous databases

EvolutionaryTraceiP16575.

Family and domain databases

Gene3Di1.10.287.130. 1 hit.
1.20.120.160. 1 hit.
3.30.565.10. 1 hit.
InterProiIPR011006. CheY-like_superfamily.
IPR003661. EnvZ-like_dim/P.
IPR003594. HATPase_C.
IPR000014. PAS.
IPR000700. PAS-assoc_C.
IPR013767. PAS_fold.
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.
IPR001638. Solute-binding_3/MltF_N.
[Graphical view]
PfamiPF02518. HATPase_c. 1 hit.
PF00512. HisKA. 1 hit.
PF01627. Hpt. 1 hit.
PF00989. PAS. 1 hit.
PF00072. Response_reg. 1 hit.
[Graphical view]
PRINTSiPR00344. BCTRLSENSOR.
SMARTiSM00387. 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]
SUPFAMiSSF47226. SSF47226. 2 hits.
SSF47384. SSF47384. 1 hit.
SSF52172. SSF52172. 1 hit.
SSF55785. SSF55785. 1 hit.
SSF55874. SSF55874. 1 hit.
TIGRFAMsiTIGR00229. sensory_box. 1 hit.
PROSITEiPS50109. HIS_KIN. 1 hit.
PS50894. HPT. 1 hit.
PS50113. PAC. 1 hit.
PS50112. PAS. 1 hit.
PS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiBVGS_BORPE
AccessioniPrimary (citable) accession number: P16575
Secondary accession number(s): P16576
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: September 19, 2003
Last modified: June 24, 2015
This is version 150 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

Was originally thought to be two separate ORFs named bvgB and bvgC.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.