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P16575

- BVGS_BORPE

UniProt

P16575 - BVGS_BORPE

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Protein
Virulence sensor protein BvgS
Gene
bvgS, BP1877
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 bindingInferred from electronic annotationi Source: UniProtKB-KW
  2. phosphorelay response regulator activityInferred from electronic annotationi Source: InterPro
  3. phosphorelay sensor kinase activityInferred from electronic annotationi Source: InterPro
  4. transporter activityInferred from electronic annotationi Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. pathogenesisInferred from electronic annotationi Source: UniProtKB-KW
  2. regulation of transcription, DNA-templatedInferred from electronic annotationi Source: InterPro
  1. phosphorelay response regulator activityInferred from electronic annotationi Source: InterPro
  2. phosphorelay sensor kinase activityInferred from electronic annotationi Source: InterPro
  3. transporter activityInferred from electronic annotationi 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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini33 – 307275Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei308 – 33124Helical; Reviewed prediction
Add
BLAST
Topological domaini332 – 541210Periplasmic Reviewed prediction
Add
BLAST
Transmembranei542 – 56322Helical; Reviewed prediction
Add
BLAST
Topological domaini564 – 1238675Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. integral component of membraneInferred from electronic annotationi Source: UniProtKB-KW
  2. plasma membraneInferred from electronic annotationi Source: UniProtKB-SubCell
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. 1 Publication
Mutagenesisi1172 – 11721H → Q: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3232 Reviewed prediction
Add
BLAST
Chaini33 – 12381206Virulence sensor protein BvgS
PRO_0000032370Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei729 – 7291Phosphohistidine; by autocatalysis Inferred
Modified residuei1023 – 102314-aspartylphosphate Inferred
Modified residuei1172 – 11721Phosphohistidine Inferred

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

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.

Miscellaneous databases

EvolutionaryTraceiP16575.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini580 – 65172PAS
Add
BLAST
Domaini652 – 70857PAC
Add
BLAST
Domaini726 – 948223Histidine kinase
Add
BLAST
Domaini974 – 1095122Response regulatory
Add
BLAST
Domaini1133 – 122896HPt
Add
BLAST

Sequence similaritiesi

Contains 1 HPt domain.

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]FASTA

« 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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti705 – 7051K → E1 Publication
Sequence conflicti705 – 7051K → E1 Publication
Sequence conflicti1068 – 10681R → A1 Publication
Sequence conflicti1068 – 10681R → A1 Publication

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...

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

« 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 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: July 9, 2014
This is version 140 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 (1 Publication) thought to be two separate ORFs named bvgB and bvgC.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

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