YVRG_BACSU
ID YVRG_BACSU Reviewed; 580 AA.
AC O34989; Q7B2K3;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Sensor histidine kinase YvrG;
DE EC=2.7.13.3;
GN Name=yvrG; OrderedLocusNames=BSU33210;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9639930; DOI=10.1099/00221287-144-6-1593;
RA Wipat A., Brignell C.S., Guy J.B., Rose M., Emmerson P.T., Harwood C.R.;
RT "The yvsA-yvqA (293 degrees - 289 degrees) region of the Bacillus subtilis
RT chromosome containing genes involved in metal ion uptake and a putative
RT sigma factor.";
RL Microbiology 144:1593-1600(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP SEQUENCE REVISION TO 394-395.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [4]
RP FUNCTION.
RX PubMed=11717295; DOI=10.1128/jb.183.24.7365-7370.2001;
RA Kobayashi K., Ogura M., Yamaguchi H., Yoshida K., Ogasawara N., Tanaka T.,
RA Fujita Y.;
RT "Comprehensive DNA microarray analysis of Bacillus subtilis two-component
RT regulatory systems.";
RL J. Bacteriol. 183:7365-7370(2001).
RN [5]
RP FUNCTION.
RX PubMed=16306698; DOI=10.1271/bbb.69.2155;
RA Serizawa M., Kodama K., Yamamoto H., Kobayashi K., Ogasawara N.,
RA Sekiguchi J.;
RT "Functional analysis of the YvrGHb two-component system of Bacillus
RT subtilis: identification of the regulated genes by DNA microarray and
RT northern blot analyses.";
RL Biosci. Biotechnol. Biochem. 69:2155-2169(2005).
CC -!- FUNCTION: Member of the two-component regulatory system YvrG/YvrH that
CC positively regulates 7 transcriptional units (wprA, wapA-yxxG,
CC dltABCDE, sunA, sunT-bdbA-yolJ-bdbB, sigO-rsoA, and sigX-rsiX), and
CC negatively regulates the lytABC operon. Probably activates YvrH by
CC phosphorylation. {ECO:0000269|PubMed:11717295,
CC ECO:0000269|PubMed:16306698}.
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 membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA11731.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ223978; CAA11731.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL009126; CAB15311.2; -; Genomic_DNA.
DR PIR; B70047; B70047.
DR RefSeq; NP_391201.2; NC_000964.3.
DR RefSeq; WP_003243980.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; O34989; -.
DR SMR; O34989; -.
DR STRING; 224308.BSU33210; -.
DR PaxDb; O34989; -.
DR PRIDE; O34989; -.
DR EnsemblBacteria; CAB15311; CAB15311; BSU_33210.
DR GeneID; 935985; -.
DR KEGG; bsu:BSU33210; -.
DR PATRIC; fig|224308.179.peg.3602; -.
DR eggNOG; COG2205; Bacteria.
DR InParanoid; O34989; -.
DR OMA; IIQFIMQ; -.
DR PhylomeDB; O34989; -.
DR BioCyc; BSUB:BSU33210-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0009927; F:histidine phosphotransfer kinase activity; IBA:GO_Central.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IBA:GO_Central.
DR GO; GO:0046777; P:protein autophosphorylation; IBA:GO_Central.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 3.30.565.10; -; 1.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..580
FT /note="Sensor histidine kinase YvrG"
FT /id="PRO_0000360787"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..261
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..282
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 283..580
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 363..580
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 366
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT CONFLICT 394..395
FT /note="VK -> GE (in Ref. 1; CAA11731)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 580 AA; 67799 MW; 5FC6D889083EADC0 CRC64;
MRLRWKFLFH FFGQMLIVIL LLTVMLVASF FYLDARFSDA ESNSGLTKAT TDTLEAYLDV
NEDGTWEVDN FLKKSVDKQH GWMQIIDSEG NTDYSYGVPK DVPGTYTKKE LLSIYKTKKL
HNYKLNYWAI NIEDKSYLLL SGWKSKSEQL LTSVEKREQK IDSLAHYKSS TIDYIKRKKG
AIYLLDSNGK ILDSINSTKS ERKTMNQLEL LKYSSKPWNY KREISVKILN KDRWMVATVP
NPVYVTDQEF NKSFLKVVLK AMFLVMAVLF MYIIWMTVWY MFRFGLPIFH TIRWLVNLSK
GKLEEPRNRE GRPVSKNKKG KIKQPYRFFG EIFESMDQLT ETLRRDKRNR EKIQATREEW
IAGLSHDLKT PLSSIYGYSM MLESKQYDWS PEEVKEMGQV VREKSEYMSK LIEDLNLTYR
LKNDALPIER KLTSLIPFFK NVIEDFKKNP FSEGYDISFV SKEEHIEFAL DEAWFRRILE
NLLGNAVKHN GKGTEIQVIL EQTKNHISLK VKDNGKGMDE ETITHLFNRY YRGTNTKDST
AGTGLGLAIA KELVHLHNGT IHVNSRTNIG TVITILFKKQ