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 27-MAR-2024, entry version 185. 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; Pseudomonadota; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PaxDb; 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 BRENDA; 2.7.13.3; 899. DR EvolutionaryTrace; P16575; -. DR PHI-base; PHI:8545; -. DR Proteomes; UP000002676; Chromosome. 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 DNA-templated transcription; IEA:InterPro. DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1. DR CDD; cd00082; HisKA; 1. DR CDD; cd00088; HPT; 1. DR CDD; cd00130; PAS; 1. DR CDD; cd13705; PBP2_BvgS_D1; 1. DR CDD; cd13707; PBP2_BvgS_D2; 1. DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1. DR Gene3D; 1.10.287.130; -; 1. DR Gene3D; 3.40.50.2300; -; 1. DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1. DR Gene3D; 1.20.120.160; HPT domain; 1. DR Gene3D; 3.30.450.20; PAS domain; 1. DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 4. 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 NCBIfam; TIGR00229; sensory_box; 1. DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1. DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1. 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; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1. DR SUPFAM; SSF52172; CheY-like; 1. DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1. DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1. DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 2. DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 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 //