BVGS_BORPA
ID BVGS_BORPA Reviewed; 1238 AA.
AC P40330;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Virulence sensor protein BvgS;
DE EC=2.7.13.3;
DE Flags: Precursor;
GN Name=bvgS; OrderedLocusNames=BPP3029;
OS Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257311;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 9305;
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=12822 / ATCC BAA-587 / NCTC 13253;
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; X52948; CAA37124.1; -; Genomic_DNA.
DR EMBL; BX640432; CAE38319.1; -; Genomic_DNA.
DR PIR; S17946; S17946.
DR RefSeq; WP_010928858.1; NC_002928.3.
DR AlphaFoldDB; P40330; -.
DR SMR; P40330; -.
DR EnsemblBacteria; CAE38319; CAE38319; BPP3029.
DR KEGG; bpa:BPP3029; -.
DR HOGENOM; CLU_000445_37_3_4; -.
DR OMA; NFGKHEA; -.
DR BRENDA; 2.7.13.3; 898.
DR Proteomes; UP000001421; 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 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..32
FT /evidence="ECO:0000255"
FT CHAIN 33..1238
FT /note="Virulence sensor protein BvgS"
FT /id="PRO_0000032369"
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 1067..1068
FT /note="QR -> HA (in Ref. 1; CAA37124)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1238 AA; 134819 MW; 3A0FBF9C5EC17246 CRC64;
MPAPHRLYPR SLICLAQALL VWALLAWAPA 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 AAEREPRFED
RDVTLHGRTR HVYQWTVPYG DSLGELKGII GGWIDITERA ELLRELHDAK ESADAANRAK
TTFLATMSHE IRTPMNAIIG MLELALLRPA DQEPDRQSIQ VAYDSARSLL ELIGDILDIA
KIEAGKFDLA PVRTALRALP EGAIRLFDGL ARQKGIELVL KTDIVGVDDV LIDPLRMKQV
LSNLVGNAIK FTTEGQVVLT VTARPDGEAA HVQFSVSDTG CGISEADQRQ LFKPFSQVGG
SAEAGPAPGT GLGLSISRRL VELMGGTLVM RSAPGVGTTV SVDLRLTMIE KSAQATPPAA
AAQATPSKPQ VSLRVLVVDD HKPNLMLLRQ QLDYLGQRVV AADSGEAALA LWHEHAFDVV
ITDCNMPGIN GYELARRIRA AEAAPGYGRT RCILFGFTAS AQMDEAQRCR AAGMDDCLFK
PIGVDALRQR LNEAAARAAL PTPPSPQAAA PATHDATPAA FSAESILALT QNDEALIRQL
LEEVIRTNRA DVDQLQKLHQ QADWPKVSDM AHRLAGGARV VDAKAMIDTA LALEKKAQGQ
AGPSPEIDGL VRTLAAQSAA LETQLRAWLE QRPHQGQP
