ID   BVGS_BORBR              Reviewed;        1238 AA.
AC   P26762;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2003, sequence version 2.
DT   27-MAR-2024, entry version 171.
DE   RecName: Full=Virulence sensor protein BvgS;
DE            EC=2.7.13.3;
DE   Flags: Precursor;
GN   Name=bvgS; OrderedLocusNames=BB2995;
OS   Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)
OS   (Alcaligenes bronchisepticus).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=7865;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-588 / NCTC 13252 / RB50;
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).
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 (By similarity). {ECO:0000250}.
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. {ECO:0000250}.
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DR   EMBL; X58355; CAA41252.1; -; Genomic_DNA.
DR   EMBL; BX640446; CAE33487.1; -; Genomic_DNA.
DR   PIR; S17944; S17944.
DR   RefSeq; WP_010926708.1; NC_002927.3.
DR   AlphaFoldDB; P26762; -.
DR   SMR; P26762; -.
DR   KEGG; bbr:BB2995; -.
DR   eggNOG; COG0834; Bacteria.
DR   eggNOG; COG2205; Bacteria.
DR   HOGENOM; CLU_000445_37_3_4; -.
DR   BRENDA; 2.7.13.3; 227.
DR   Proteomes; UP000001027; 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   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Kinase; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Signal; Transferase; Transmembrane;
KW   Transmembrane helix; Two-component regulatory system; Virulence.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..1238
FT                   /note="Virulence sensor protein BvgS"
FT                   /id="PRO_0000032368"
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:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         1023
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   MOD_RES         1172
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00110"
FT   CONFLICT        50
FT                   /note="A -> T (in Ref. 1; CAA41252)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        395
FT                   /note="M -> L (in Ref. 1; CAA41252)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        651
FT                   /note="S -> A (in Ref. 1; CAA41252)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1008
FT                   /note="A -> S (in Ref. 1; CAA41252)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1067..1068
FT                   /note="QR -> HA (in Ref. 1; CAA41252)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1144
FT                   /note="L -> V (in Ref. 1; CAA41252)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1238 AA;  134811 MW;  74DCB538B77A0F3E CRC64;
     MPAPHRLYPR SLICLAQALL AWALLAWAPA QASQELTLVG KAAVPDVEIA LDGDDWRWLA
     RKRVLTLGVY APDIPPFDVT YDERYEGLTA DYMAIIAHNL GVQAKVLRYP TREQAVGALE
     SGQIDLIGTV NGIEGRLQSL RLSVPYAADH PVLVMPIGAR RAPPADLAGQ RLAVDANYLP
     RETLQQAYPQ ATLHYFPSSE QALAAVAYGQ ADVFIGDALT TSHLVSQSYF NDVRVVAPAQ
     IVTGGESFGV RADNTRLLRV VNAVLEAIPA SERRSLIYRW GLGSSISLDF ARPAYSAREQ
     QWMANHPVVK VAVLNLFAPF TLFRTDEQFG GISAAVLQLL QLRTGLDFQI IGVDTVEELI
     AKLRSGEADM AGALFVNAAR ESVLSFSRPY VRNGMVIVTR QDPAAPADAD HLDGRTIAMV
     RNSAAIPLLQ QRYPQAKVVT ADNPTEAMLL VADGQADAVV QTQISASYYV NRYFAGKLRI
     ASALDLPPAE IALATARGQT ELISILNKAL YSISNDELAS IVSRWRGSDG DPRTWYAYRN
     EIYLLIGLGL LSALLFLSWI VYLRRQIRQR KRAERALNDQ LEFMRVLIDG TPNPIYVRDK
     EGRMLLCNDA YLDTFGVTAD AVLGKTIPEA NVVGDPALAR EMHEFLLTRM SAEREPRFED
     RDVTLHGRTR HVYQWTVPYG DSLGELKGII GGWIDITERA ELLRELHDAK ESADAANRAK
     TTFLATMSHE IRTPMNAIIG MLELALLRPA DQEPDRQSIQ VAYDSARSLL ELIGDILDIA
     KIEAGKFDLA PVRTALRALP EGAIRVFDGL ARQKGIELVL KTDIVGVDDV LIDPLRMKQV
     LSNLVGNAIK FTTEGQVVLT VTARPDGEAA HVQFSVSDTG CGISEADQRQ LFKPFSQVGG
     SAEAGPAPGT GLGLSISRRL VELMGGTLVM RSAPGVGTTV SVDLRLTMVE KSAQATPPAA
     AAQATPSKPQ VSLRVLVVDD HKPNLMLLRQ QLDYLGQRVV AADSGEAALA LWHEHAFDVV
     ITDCNMPGIN GYELARRIRA AEAAPGYGRT RCILFGFTAS AQMDEAQRCR AAGMDDCLFK
     PIGVDALRQR LNEAAARAAL PTPPSPQAAA PATHDATPAA FSAESILALT QNDEALIRQL
     LEELIRTNRA DVDQLQKLHQ QADWPKVSDM AHRLAGGARV VDAKAMIDTA LALEKKAQGQ
     AGPSPEIDGM VRTLAAQSAA LETQLRAWLE QRPHQGQP
//