P16575 (BVGS_BORPE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Virulence sensor protein BvgS
EC=2.7.13.3

Gene names

Name:	bvgS
Ordered Locus Names:	BP1877

Organism

Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251) [Reference proteome] [HAMAP]

Taxonomic identifier

257313 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella › Bordetella pertussis

Protein attributes

Sequence length	1238 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Two-component regulatory system Virulence
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Signal Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	intracellular signal transduction Inferred from electronic annotation. Source: GOC pathogenesis Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro signal transduction by phosphorylation Inferred from electronic annotation. Source: GOC
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW outer membrane-bounded periplasmic space Inferred from electronic annotation. Source: InterPro plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW phosphorelay response regulator activity Inferred from electronic annotation. Source: InterPro phosphorelay sensor kinase activity Inferred from electronic annotation. Source: InterPro transporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 32

32

Potential

Chain

33 – 1238

1206

Virulence sensor protein BvgS

PRO_0000032370

Regions

Topological domain

33 – 307

275

Cytoplasmic Potential

Transmembrane

308 – 331

24

Helical; Potential

Topological domain

332 – 541

210

Periplasmic Potential

Transmembrane

542 – 563

22

Helical; Potential

Topological domain

564 – 1238

675

Cytoplasmic Potential

Domain

580 – 651

72

PAS

Domain

652 – 708

57

PAC

Domain

726 – 948

223

Histidine kinase

Domain

974 – 1095

122

Response regulatory

Domain

1133 – 1228

96

HPt

Amino acid modifications

Modified residue

729

1

Phosphohistidine; by autocatalysis Probable

Modified residue

1023

1

4-aspartylphosphate Probable

Modified residue

1172

1

Phosphohistidine Probable

Experimental info

Mutagenesis

729

1

H → Q: Loss of autophosphorylation. Ref.5

Mutagenesis

979

1

D → G: Loss of activity; when associated with G-980. Ref.6

Mutagenesis

980

1

D → G: Loss of activity. Ref.6

Mutagenesis

1023

1

D → G or N: Loss of activity. Ref.5 Ref.6

Mutagenesis

1080

1

K → L: Loss of activity. Ref.6

Mutagenesis

1146 – 1147

2

Missing: Loss of activity. Ref.6

Mutagenesis

1172

1

H → Q: Loss of activity. Ref.7

Sequence conflict

705

1

K → E Ref.1

Sequence conflict

705

1

K → E Ref.2

Sequence conflict

1068

1

R → A Ref.1

Sequence conflict

1068

1

R → A Ref.2

Secondary structure

1

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1238

Helix Strand Turn

Details...

Helix

297 – 305

9

Beta strand

307 – 314

8

Turn

318 – 320

3

Beta strand

321 – 323

3

Beta strand

329 – 331

3

Helix

332 – 344

13

Beta strand

347 – 355

9

Helix

356 – 365

10

Beta strand

369 – 375

7

Helix

378 – 380

3

Turn

381 – 383

3

Beta strand

384 – 386

3

Beta strand

390 – 393

4

Beta strand

395 – 402

8

Helix

409 – 411

3

Beta strand

416 – 420

5

Helix

425 – 432

8

Beta strand

436 – 443

8

Helix

444 – 452

9

Beta strand

457 – 462

6

Helix

463 – 473

11

Turn

475 – 477

3

Beta strand

478 – 483

6

Beta strand

489 – 496

8

Helix

500 – 511

12

Helix

515 – 523

9

Sequences

	Sequence		Length	Mass (Da)
	P16575 [UniParc]. Last modified September 19, 2003. Version 3. Checksum: 28433439765ABC66	FASTA	1,238	135,001
	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

References

	« Hide 'large scale' referencesShow '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. , 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.

PIR

A40185.

RefSeq

NP_880569.1. NC_002929.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3MPK	X-ray	2.04	A	287-541	[»]
3MPL	X-ray	2.10	A	287-542	[»]

ProteinModelPortal

P16575.

ModBase

Search...

Protein-protein interaction databases

STRING

257313.BP1877.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

CAE42160; CAE42160; BP1877.

GeneID

2667057.

KEGG

bpe:BP1877.

PATRIC

21157042. VBIBorPer7866_2016.

Phylogenomic databases

eggNOG

COG0642.

HOGENOM

HOG000269369.

KO

K07679.

OMA

SFAEAFI.

ProtClustDB

CLSK920529.

Enzyme and pathway databases

BioCyc

BPER257313:BP1877-MONOMER.

BRENDA

2.7.13.3. 899.

Family and domain databases

Gene3D

1.10.287.130. 1 hit.
1.20.120.160. 1 hit.
3.30.565.10. 1 hit.

InterPro

IPR011006. CheY-like_superfamily.
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.
IPR003661. Sig_transdc_His_kin_sub1_dim/P.
IPR005467. Sig_transdc_His_kinase_core.
IPR009082. Sig_transdc_His_kinase_dimeric.
IPR001789. Sig_transdc_resp-reg_receiver.
[Graphical view]

Pfam

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]

PRINTS

PR00344. BCTRLSENSOR.

SMART

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]

SUPFAM

SSF55874. ATP_bd_ATPase. 1 hit.
SSF52172. CheY_like. 1 hit.
SSF47384. His_kin_homodim. 1 hit.
SSF47226. Hpt. 1 hit.

TIGRFAMs

TIGR00229. sensory_box. 1 hit.

PROSITE

PS50109. HIS_KIN. 1 hit.
PS50894. HPT. 1 hit.
PS50113. PAC. 1 hit.
PS50112. PAS. 1 hit.
PS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P16575.

Entry information

Entry name

BVGS_BORPE

Accession

Primary (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:	May 1, 2013
This is version 131 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program