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P16575

- BVGS_BORPE

UniProt

P16575 - BVGS_BORPE

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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: 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

  1. ATP binding Source: UniProtKB-KW
  2. phosphorelay sensor kinase activity Source: InterPro
  3. transporter activity Source: InterPro

GO - Biological processi

  1. pathogenesis Source: UniProtKB-KW
  2. regulation of transcription, DNA-templated Source: InterPro
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: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-KW
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
Helixi297 – 3059
Beta strandi307 – 3148
Turni318 – 3203
Beta strandi321 – 3233
Beta strandi329 – 3313
Helixi332 – 34413
Beta strandi347 – 3559
Helixi356 – 36510
Beta strandi369 – 3757
Helixi378 – 3803
Turni381 – 3833
Beta strandi384 – 3863
Beta strandi390 – 3934
Beta strandi395 – 4028
Helixi409 – 4113
Beta strandi416 – 4205
Helixi425 – 4328
Beta strandi436 – 4438
Helixi444 – 4529
Beta strandi457 – 4626
Helixi463 – 47311
Turni475 – 4773
Beta strandi478 – 4836
Beta strandi489 – 4968
Helixi500 – 51112
Helixi515 – 5239

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3MPKX-ray2.04A287-542[»]
3MPLX-ray2.10A287-542[»]
ProteinModelPortaliP16575.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16575.

Topological domain

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

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei308 – 33124HelicalSequence AnalysisAdd
BLAST
Transmembranei542 – 56322HelicalSequence AnalysisAdd
BLAST

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.
OMAiAPAHIAT.
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.
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]
PfamiPF02518. 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]
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 [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:
EMBL
GenBank
DDBJ
Links Updated
M25401 Genomic DNA. Translation: AAA22970.1.
BX640416 Genomic DNA. Translation: CAE42160.1.
PIRiA40185.
RefSeqiNP_880569.1. NC_002929.2.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M25401 Genomic DNA. Translation: AAA22970.1 .
BX640416 Genomic DNA. Translation: CAE42160.1 .
PIRi A40185.
RefSeqi NP_880569.1. NC_002929.2.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3MPK X-ray 2.04 A 287-542 [» ]
3MPL X-ray 2.10 A 287-542 [» ]
ProteinModelPortali P16575.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 257313.BP1877.

Proteomic databases

PRIDEi P16575.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAE42160 ; CAE42160 ; BP1877 .
GeneIDi 2667057.
KEGGi bpe:BP1877.
PATRICi 21157042. VBIBorPer7866_2016.

Phylogenomic databases

eggNOGi COG0642.
HOGENOMi HOG000269369.
KOi K07679.
OMAi APAHIAT.
OrthoDBi EOG6G4VQG.

Enzyme and pathway databases

BioCyci BPER257313:BP1877-MONOMER.
BRENDAi 2.7.13.3. 899.

Miscellaneous databases

EvolutionaryTracei P16575.

Family and domain databases

Gene3Di 1.10.287.130. 1 hit.
1.20.120.160. 1 hit.
3.30.565.10. 1 hit.
InterProi IPR011006. CheY-like_superfamily.
IPR003661. EnvZ-like_dim/P.
IPR003594. HATPase_C.
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 ]
Pfami PF02518. 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 ]
PRINTSi PR00344. BCTRLSENSOR.
SMARTi SM00387. 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 ]
SUPFAMi SSF47226. SSF47226. 2 hits.
SSF47384. SSF47384. 1 hit.
SSF52172. SSF52172. 1 hit.
SSF55785. SSF55785. 1 hit.
SSF55874. SSF55874. 1 hit.
TIGRFAMsi TIGR00229. sensory_box. 1 hit.
PROSITEi PS50109. HIS_KIN. 1 hit.
PS50894. HPT. 1 hit.
PS50113. PAC. 1 hit.
PS50112. PAS. 1 hit.
PS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 143 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