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P16575

- BVGS_BORPE

UniProt

P16575 - BVGS_BORPE

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
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 3 (19 Sep 2003)
      Previous versions | rss
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    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 response regulator activity Source: InterPro
    3. phosphorelay sensor kinase activity Source: InterPro
    4. transporter activity Source: InterPro

    GO - Biological processi

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

    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-SubCell

    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. 1 Publication
    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_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]
    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.

    P16575-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPAPHRLYPR SLICLAQALL AWALLAWAPA QASQELTLVG KAAVPDVEVA     50
    LDGDDWRWLA RKRVLTLGVY APDIPPFDVT YGERYEGLTA DYMAIIAHNL 100
    GMQAKVLRYP TREQALSALE SGQIDLIGTV NGTDGRQQSL RLSVPYAADH 150
    PVIVMPIGAR HVPASNLAGQ RLAVDINYLP KETLARAYPQ ATLHYFPSSE 200
    QALAAVAYGQ ADVFIGDALT TSHLVSQSYF NDVRVVAPAH IATGGESFGV 250
    RADNTRLLRV VNAVLEAIPP SEHRSLIYRW GLGSSISLDF AHPAYSAREQ 300
    QWMADHPVVK VAVLNLFAPF TLFRTDEQFG GISAAVLQLL QLRTGLDFEI 350
    IGVDTVEELI AKLRSGEADM AGALFVNSAR ESFLSFSRPY VRNGMVIVTR 400
    QDPDAPVDAD HLDGRTVALV RNSAAIPLLQ RRYPQAKVVT ADNPSEAMLM 450
    VANGQADAVV QTQISASYYV NRYFAGKLRI ASALDLPPAE IALATTRGQT 500
    ELMSILNKAL YSISNDELAS IISRWRGSDG DPRTWYAYRN EIYLLIGLGL 550
    LSALLFLSWI VYLRRQIRQR KRAERALNDQ LEFMRVLIDG TPNPIYVRDK 600
    EGRMLLCNDA YLDTFGVTAD AVLGKTIPEA NVVGDPALAR EMHEFLLTRV 650
    AAEREPRFED RDVTLHGRTR HVYQWTIPYG DSLGELKGII GGWIDITERA 700
    ELLRKLHDAK ESADAANRAK TTFLATMSHE IRTPMNAIIG MLELALLRPT 750
    DQEPDRQSIQ VAYDSARSLL ELIGDILDIA KIEAGKFDLA PVRTALRVLP 800
    EGAIRVFDGL ARQKGIELVL KTDIVGVDDV LIDPLRMKQV LSNLVGNAIK 850
    FTTEGQVVLA VTARPDGDAA HVQFSVSDTG CGISEADQRQ LFKPFSQVGG 900
    SAEAGPAPGT GLGLSISRRL VELMGGTLVM RSAPGVGTTV SVDLRLTMVE 950
    KSVQAAPPAA ATAATPSKPQ VSLRVLVVDD HKPNLMLLRQ QLDYLGQRVI 1000
    AADSGEAALA LWREHAFDVV ITDCNMPGIS GYELARRIRA AEAAPGYGRT 1050
    RCILFGFTAS AQMDEAQRCR AAGMDDCLFK PIGVDALRQR LNEAVARAAL 1100
    PTPPSPQAAA PATDDATPTA FSAESILALT QNDEALIRQL LEEVIRTNRA 1150
    DVDQLQKLHQ QADWPKVSDM AHRLAGGARV VDAKAMIDTV LALEKKAQGQ 1200
    AGPSPEIDGL VRTLAAQSAA LETQLRAWLE QRPHQDQP 1238
    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.
    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:
    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.
    WP_010930608.1. 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_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 ]
    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

    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 1, 2014
    This is version 142 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