ID BVGS_BORPE STANDARD; PRT; 1238 AA. AC P16575; P16576; DT 01-AUG-1990 (Rel. 15, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Virulence sensor protein bvgS precursor (EC 2.7.3.-). GN BVGS OR BP1877. OS Bordetella pertussis. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Bordetella. OX NCBI_TaxID=520; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89367311; PubMed=2549542; 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 RT proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 86:6671-6675(1989). RN [2] RP REVISIONS, SEQUENCE FROM N.A. RX MEDLINE=92167813; PubMed=1791760; RA Arico B., Scarlato V., Monack D.M., Falkow S., Rappuoli R.; RT "Structural and genetic analysis of the bvg locus in Bordetella RT species."; RL Mol. Microbiol. 5:2481-2491(1991). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251; RX MEDLINE=22827954; PubMed=12910271; RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N., 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., 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., RA Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., RA Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., RA Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., RA Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., RA Unwin L., Whitehead S., 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 MUTAGENESIS OF HIS-729 AND ASP-1023. RX MEDLINE=94134718; PubMed=8302847; RA Uhl M.A., Miller J.F.; RT "Autophosphorylation and phosphotransfer in the Bordetella pertussis RT BvgAS signal transduction cascade."; RL Proc. Natl. Acad. Sci. U.S.A. 91:1163-1167(1994). RN [5] RP MUTAGENESIS OF ASP-979; ASP-980; ASP-1023; LYS-1080; ARG-1146 AND RP THR-1147. RC STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251; RX MEDLINE=95271651; PubMed=7752227; 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 [6] RP CHARACTERIZATION, AND MUTAGENESIS OF HIS-1172. RX MEDLINE=96183187; PubMed=8605872; RA Uhl M.A., Miller J.F.; RT "Integration of multiple domains in a two-component sensor protein: RT the Bordetella pertussis BvgAS phosphorelay."; RL EMBO J. 15:1028-1036(1996). RN [7] RP CHARACTERIZATION. RX MEDLINE=98194702; PubMed=9535079; RA Perraud A.-L., Kimmel B., Weiss V., Gross R.; RT "Specificity of the BvgAS and EvgAS phosphorelay is mediated by the RT C-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 -!- SUBCELLULAR LOCATION: Integral membrane protein. Inner membrane CC (Probable). CC -!- PTM: Activation requires a sequential transfer of a phosphate CC group from a His in the primary transmitter domain, to an Asp in CC the receiver domain and to a His in the secondary transmitter CC domain. CC -!- SIMILARITY: Contains 1 histidine kinase domain. CC -!- SIMILARITY: Contains 1 HPt domain. CC -!- SIMILARITY: Contains 1 PAS (PER-ARNT-SIM) dimerization domain. CC -!- SIMILARITY: Contains 1 PAS-associated C-terminal (PAC) domain. CC -!- SIMILARITY: Contains 1 response regulatory domain. CC -!- CAUTION: Was originally (Ref.1) thought to be two separate ORFs CC named bvgB and bvgC. 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; -. DR EMBL; BX640416; CAE42160.1; -. DR PIR; A40185; A40185. DR InterPro; IPR003594; ATPbind_ATPase. DR InterPro; IPR004358; Bact_sens_pr_C. DR InterPro; IPR003661; His_kinA_N. DR InterPro; IPR005467; His_kinase. DR InterPro; IPR008207; Hpt. DR InterPro; IPR000700; PAS-assoc_C. DR InterPro; IPR000014; PAS_domain. DR InterPro; IPR001789; Response_reg. DR InterPro; IPR001311; SBP/glu_receptor. DR InterPro; IPR001638; SBP_bac_3. DR Pfam; PF02518; HATPase_c; 1. DR Pfam; PF00512; HisKA; 1. DR Pfam; PF00989; PAS; 1. DR Pfam; PF00072; response_reg; 1. DR Pfam; PF00497; SBP_bac_3; 2. DR PRINTS; PR00344; BCTRLSENSOR. DR ProDom; PD000039; Response_reg; 1. 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 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. KW Sensory transduction; Transferase; Kinase; Phosphorylation; KW Transmembrane; Inner membrane; Signal; Complete proteome. FT SIGNAL 1 32 Potential. FT CHAIN 33 1238 Virulence sensor protein bvgS. FT DOMAIN 33 307 Cytoplasmic (Potential). FT TRANSMEM 308 331 Potential. FT DOMAIN 332 541 Periplasmic (Potential). FT TRANSMEM 542 563 Potential. FT DOMAIN 564 1238 Cytoplasmic (Potential). FT DOMAIN 580 651 PAS. FT DOMAIN 652 708 PAC. FT DOMAIN 726 948 Histidine kinase. FT DOMAIN 974 1095 Response regulatory. FT DOMAIN 1133 1228 HPt. FT MOD_RES 729 729 PHOSPHORYLATION (AUTO-) (PROBABLE). FT MOD_RES 1023 1023 PHOSPHORYLATION (PROBABLE). FT MOD_RES 1172 1172 PHOSPHORYLATION (PROBABLE). FT MUTAGEN 729 729 H->Q: LOSS OF AUTOPHOSPHORYLATION. FT MUTAGEN 979 979 D->G: LOSS OF ACTIVITY; WHEN ASSOCIATED FT WITH G-980. FT MUTAGEN 980 980 D->G: LOSS OF ACTIVITY. FT MUTAGEN 1023 1023 D->G,N: LOSS OF ACTIVITY. FT MUTAGEN 1080 1080 K->L: LOSS OF ACTIVITY. FT MUTAGEN 1146 1147 Missing: Loss of activity. FT MUTAGEN 1172 1172 H->Q: Loss of activity. FT CONFLICT 705 705 K -> E (in Ref. 1 and 2). FT CONFLICT 1068 1068 R -> A (in Ref. 1 and 2). SQ SEQUENCE 1238 AA; 135000 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 //