BVGS_BORPE
ID BVGS_BORPE Reviewed; 1238 AA.
AC P16575; P16576;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2003, sequence version 3.
DT 25-MAY-2022, entry version 178.
DE RecName: Full=Virulence sensor protein BvgS;
DE EC=2.7.13.3;
DE Flags: Precursor;
GN Name=bvgS; OrderedLocusNames=BP1877;
OS Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257313;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2549542; DOI=10.1073/pnas.86.17.6671;
RA Arico B., Miller J.F., Roy C., Stibitz S., Monack D.M., Falkow S.,
RA Gross R., Rappuoli R.;
RT "Sequences required for expression of Bordetella pertussis virulence
RT factors share homology with prokaryotic signal transduction proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:6671-6675(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION.
RX PubMed=1791760; DOI=10.1111/j.1365-2958.1991.tb02093.x;
RA Arico B., Scarlato V., Monack D.M., Falkow S., Rappuoli R.;
RT "Structural and genetic analysis of the bvg locus in Bordetella species.";
RL Mol. Microbiol. 5:2481-2491(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
RX PubMed=12910271; DOI=10.1038/ng1227;
RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA Barrell B.G., Maskell D.J.;
RT "Comparative analysis of the genome sequences of Bordetella pertussis,
RT Bordetella parapertussis and Bordetella bronchiseptica.";
RL Nat. Genet. 35:32-40(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 827-1153.
RX PubMed=2537932; DOI=10.1038/338266a0;
RA Stibitz S., Aaronson W., Monack D., Falkow S.;
RT "Phase variation in Bordetella pertussis by frameshift mutation in a gene
RT for a novel two-component system.";
RL Nature 338:266-269(1989).
RN [5]
RP MUTAGENESIS OF HIS-729 AND ASP-1023.
RX PubMed=8302847; DOI=10.1073/pnas.91.3.1163;
RA Uhl M.A., Miller J.F.;
RT "Autophosphorylation and phosphotransfer in the Bordetella pertussis BvgAS
RT signal transduction cascade.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:1163-1167(1994).
RN [6]
RP MUTAGENESIS OF ASP-979; ASP-980; ASP-1023; LYS-1080; ARG-1146 AND THR-1147.
RC STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
RX PubMed=7752227; DOI=10.1006/jmbi.1995.0245;
RA Beier D., Schwarz B., Fuchs T.M., Gross R.;
RT "In vivo characterization of the unorthodox BvgS two-component sensor
RT protein of Bordetella pertussis.";
RL J. Mol. Biol. 248:596-610(1995).
RN [7]
RP CHARACTERIZATION, AND MUTAGENESIS OF HIS-1172.
RX PubMed=8605872; DOI=10.1002/j.1460-2075.1996.tb00440.x;
RA Uhl M.A., Miller J.F.;
RT "Integration of multiple domains in a two-component sensor protein: the
RT Bordetella pertussis BvgAS phosphorelay.";
RL EMBO J. 15:1028-1036(1996).
RN [8]
RP CHARACTERIZATION.
RX PubMed=9535079; DOI=10.1046/j.1365-2958.1998.00716.x;
RA Perraud A.-L., Kimmel B., Weiss V., Gross R.;
RT "Specificity of the BvgAS and EvgAS phosphorelay is mediated by the C-
RT terminal HPt domains of the sensor proteins.";
RL Mol. Microbiol. 27:875-887(1998).
CC -!- FUNCTION: Member of the two-component regulatory system BvgS/BvgA.
CC Phosphorylates BvgA via a four-step phosphorelay in response to
CC environmental signals.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- PTM: Activation requires a sequential transfer of a phosphate group
CC from a His in the primary transmitter domain, to an Asp in the receiver
CC domain and to a His in the secondary transmitter domain.
CC -!- CAUTION: Was originally thought to be two separate ORFs named bvgB and
CC bvgC. {ECO:0000305|PubMed:2549542}.
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DR EMBL; M25401; AAA22970.1; -; Genomic_DNA.
DR EMBL; BX640416; CAE42160.1; -; Genomic_DNA.
DR PIR; A40185; A40185.
DR RefSeq; NP_880569.1; NC_002929.2.
DR RefSeq; WP_010930608.1; NZ_CP039022.1.
DR PDB; 3MPK; X-ray; 2.04 A; A=287-542.
DR PDB; 3MPL; X-ray; 2.10 A; A=287-542.
DR PDB; 4Q0C; X-ray; 3.10 A; A/B/C/D=30-544.
DR PDBsum; 3MPK; -.
DR PDBsum; 3MPL; -.
DR PDBsum; 4Q0C; -.
DR AlphaFoldDB; P16575; -.
DR SMR; P16575; -.
DR STRING; 257313.BP1877; -.
DR KEGG; bpe:BP1877; -.
DR PATRIC; fig|257313.5.peg.2016; -.
DR eggNOG; COG0834; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_37_3_4; -.
DR OMA; NFGKHEA; -.
DR BRENDA; 2.7.13.3; 899.
DR EvolutionaryTrace; P16575; -.
DR PHI-base; PHI:8545; -.
DR Proteomes; UP000002676; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00088; HPT; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.20.120.160; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR036641; HPT_dom_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR001638; Solute-binding_3/MltF_N.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF00497; SBP_bac_3; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00091; PAS; 1.
DR SMART; SM00062; PBPb; 2.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF47226; SSF47226; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR SUPFAM; SSF55785; SSF55785; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR TIGRFAMs; TIGR00229; sensory_box; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell inner membrane; Cell membrane; Kinase;
KW Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome; Signal;
KW Transferase; Transmembrane; Transmembrane helix;
KW Two-component regulatory system; Virulence.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..1238
FT /note="Virulence sensor protein BvgS"
FT /id="PRO_0000032370"
FT TOPO_DOM 33..307
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 308..331
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 332..541
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 542..563
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 564..1238
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 580..651
FT /note="PAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 652..708
FT /note="PAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT DOMAIN 726..948
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 974..1095
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DOMAIN 1133..1228
FT /note="HPt"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00110"
FT MOD_RES 729
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000305"
FT MOD_RES 1023
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000305"
FT MOD_RES 1172
FT /note="Phosphohistidine"
FT /evidence="ECO:0000305"
FT MUTAGEN 729
FT /note="H->Q: Loss of autophosphorylation."
FT /evidence="ECO:0000269|PubMed:8302847"
FT MUTAGEN 979
FT /note="D->G: Loss of activity; when associated with G-980."
FT /evidence="ECO:0000269|PubMed:7752227"
FT MUTAGEN 980
FT /note="D->G: Loss of activity."
FT /evidence="ECO:0000269|PubMed:7752227"
FT MUTAGEN 1023
FT /note="D->G,N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:7752227,
FT ECO:0000269|PubMed:8302847"
FT MUTAGEN 1080
FT /note="K->L: Loss of activity."
FT /evidence="ECO:0000269|PubMed:7752227"
FT MUTAGEN 1146..1147
FT /note="Missing: Loss of activity."
FT MUTAGEN 1172
FT /note="H->Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:8605872"
FT CONFLICT 705
FT /note="K -> E (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 1068
FT /note="R -> A (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:4Q0C"
FT HELIX 54..62
FT /evidence="ECO:0007829|PDB:4Q0C"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:4Q0C"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:4Q0C"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:4Q0C"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:4Q0C"
FT HELIX 88..99
FT /evidence="ECO:0007829|PDB:4Q0C"
FT STRAND 103..111
FT /evidence="ECO:0007829|PDB:4Q0C"
FT HELIX 112..120
FT /evidence="ECO:0007829|PDB:4Q0C"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:4Q0C"
FT STRAND 134..137
FT /evidence="ECO:0007829|PDB:4Q0C"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:4Q0C"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:4Q0C"
FT HELIX 164..167
FT /evidence="ECO:0007829|PDB:4Q0C"
FT STRAND 170..175
FT /evidence="ECO:0007829|PDB:4Q0C"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:4Q0C"
FT HELIX 181..187
FT /evidence="ECO:0007829|PDB:4Q0C"
FT STRAND 191..198
FT /evidence="ECO:0007829|PDB:4Q0C"
FT HELIX 199..207
FT /evidence="ECO:0007829|PDB:4Q0C"
FT STRAND 212..217
FT /evidence="ECO:0007829|PDB:4Q0C"
FT HELIX 218..228
FT /evidence="ECO:0007829|PDB:4Q0C"
FT TURN 229..232
FT /evidence="ECO:0007829|PDB:4Q0C"
FT STRAND 233..238
FT /evidence="ECO:0007829|PDB:4Q0C"
FT STRAND 246..251
FT /evidence="ECO:0007829|PDB:4Q0C"
FT HELIX 255..267
FT /evidence="ECO:0007829|PDB:4Q0C"
FT HELIX 270..279
FT /evidence="ECO:0007829|PDB:4Q0C"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:4Q0C"
FT TURN 286..288
FT /evidence="ECO:0007829|PDB:4Q0C"
FT HELIX 297..305
FT /evidence="ECO:0007829|PDB:3MPK"
FT STRAND 307..314
FT /evidence="ECO:0007829|PDB:3MPK"
FT TURN 318..320
FT /evidence="ECO:0007829|PDB:3MPK"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:3MPL"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:3MPL"
FT HELIX 332..344
FT /evidence="ECO:0007829|PDB:3MPK"
FT STRAND 347..355
FT /evidence="ECO:0007829|PDB:3MPK"
FT HELIX 356..365
FT /evidence="ECO:0007829|PDB:3MPK"
FT STRAND 369..375
FT /evidence="ECO:0007829|PDB:3MPK"
FT HELIX 378..380
FT /evidence="ECO:0007829|PDB:3MPK"
FT TURN 381..383
FT /evidence="ECO:0007829|PDB:3MPK"
FT STRAND 384..386
FT /evidence="ECO:0007829|PDB:3MPK"
FT STRAND 390..393
FT /evidence="ECO:0007829|PDB:3MPK"
FT STRAND 395..402
FT /evidence="ECO:0007829|PDB:3MPK"
FT HELIX 409..411
FT /evidence="ECO:0007829|PDB:3MPK"
FT STRAND 416..420
FT /evidence="ECO:0007829|PDB:3MPK"
FT HELIX 425..432
FT /evidence="ECO:0007829|PDB:3MPK"
FT STRAND 436..443
FT /evidence="ECO:0007829|PDB:3MPK"
FT HELIX 444..452
FT /evidence="ECO:0007829|PDB:3MPK"
FT STRAND 457..462
FT /evidence="ECO:0007829|PDB:3MPK"
FT HELIX 463..473
FT /evidence="ECO:0007829|PDB:3MPK"
FT TURN 475..477
FT /evidence="ECO:0007829|PDB:3MPK"
FT STRAND 478..483
FT /evidence="ECO:0007829|PDB:3MPK"
FT STRAND 489..496
FT /evidence="ECO:0007829|PDB:3MPK"
FT HELIX 500..511
FT /evidence="ECO:0007829|PDB:3MPK"
FT HELIX 515..523
FT /evidence="ECO:0007829|PDB:3MPK"
FT HELIX 532..544
FT /evidence="ECO:0007829|PDB:4Q0C"
SQ SEQUENCE 1238 AA; 135001 MW; 28433439765ABC66 CRC64;
MPAPHRLYPR SLICLAQALL AWALLAWAPA QASQELTLVG KAAVPDVEVA LDGDDWRWLA
RKRVLTLGVY APDIPPFDVT YGERYEGLTA DYMAIIAHNL GMQAKVLRYP TREQALSALE
SGQIDLIGTV NGTDGRQQSL RLSVPYAADH PVIVMPIGAR HVPASNLAGQ RLAVDINYLP
KETLARAYPQ ATLHYFPSSE QALAAVAYGQ ADVFIGDALT TSHLVSQSYF NDVRVVAPAH
IATGGESFGV RADNTRLLRV VNAVLEAIPP SEHRSLIYRW GLGSSISLDF AHPAYSAREQ
QWMADHPVVK VAVLNLFAPF TLFRTDEQFG GISAAVLQLL QLRTGLDFEI IGVDTVEELI
AKLRSGEADM AGALFVNSAR ESFLSFSRPY VRNGMVIVTR QDPDAPVDAD HLDGRTVALV
RNSAAIPLLQ RRYPQAKVVT ADNPSEAMLM VANGQADAVV QTQISASYYV NRYFAGKLRI
ASALDLPPAE IALATTRGQT ELMSILNKAL YSISNDELAS IISRWRGSDG DPRTWYAYRN
EIYLLIGLGL LSALLFLSWI VYLRRQIRQR KRAERALNDQ LEFMRVLIDG TPNPIYVRDK
EGRMLLCNDA YLDTFGVTAD AVLGKTIPEA NVVGDPALAR EMHEFLLTRV AAEREPRFED
RDVTLHGRTR HVYQWTIPYG DSLGELKGII GGWIDITERA ELLRKLHDAK ESADAANRAK
TTFLATMSHE IRTPMNAIIG MLELALLRPT DQEPDRQSIQ VAYDSARSLL ELIGDILDIA
KIEAGKFDLA PVRTALRVLP EGAIRVFDGL ARQKGIELVL KTDIVGVDDV LIDPLRMKQV
LSNLVGNAIK FTTEGQVVLA VTARPDGDAA HVQFSVSDTG CGISEADQRQ LFKPFSQVGG
SAEAGPAPGT GLGLSISRRL VELMGGTLVM RSAPGVGTTV SVDLRLTMVE KSVQAAPPAA
ATAATPSKPQ VSLRVLVVDD HKPNLMLLRQ QLDYLGQRVI AADSGEAALA LWREHAFDVV
ITDCNMPGIS GYELARRIRA AEAAPGYGRT RCILFGFTAS AQMDEAQRCR AAGMDDCLFK
PIGVDALRQR LNEAVARAAL PTPPSPQAAA PATDDATPTA FSAESILALT QNDEALIRQL
LEEVIRTNRA DVDQLQKLHQ QADWPKVSDM AHRLAGGARV VDAKAMIDTV LALEKKAQGQ
AGPSPEIDGL VRTLAAQSAA LETQLRAWLE QRPHQDQP
