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Q45614

- YYCG_BACSU

UniProt

Q45614 - YYCG_BACSU

Protein

Sensor histidine kinase YycG

Gene

yycG

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Member of the two-component regulatory system YycG/YycF involved in the regulation of the ftsAZ operon, the yocH and ykvT, cwlO, lytE, ydjM, yjeA, yoeB genes and the tagAB and tagDEF operons. Probably phosphorylates YycF.3 Publications

    Catalytic activityi

    ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. phosphorelay sensor kinase activity Source: InterPro

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Two-component regulatory system

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciBSUB:BSU40400-MONOMER.
    BRENDAi2.7.13.3. 700.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sensor histidine kinase YycG (EC:2.7.13.3)
    Gene namesi
    Name:yycG
    Ordered Locus Names:BSU40400
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU40400.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi386 – 3861H → R or A: Loss of phosphorylation. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 611611Sensor histidine kinase YycGPRO_0000074918Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei386 – 3861Phosphohistidine; by autocatalysisCurated

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ45614.

    Expressioni

    Developmental stagei

    Expressed during exponential growth and shut down at the entry into stationary phase.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with YycH and YycI.1 Publication

    Protein-protein interaction databases

    IntActiQ45614. 2 interactions.
    STRINGi224308.BSU40400.

    Structurei

    Secondary structure

    1
    611
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi451 – 4533
    Helixi454 – 46613
    Beta strandi475 – 4784
    Beta strandi485 – 4884
    Helixi490 – 50617
    Beta strandi514 – 5218
    Turni522 – 5254
    Beta strandi526 – 5327
    Turni540 – 5478
    Helixi567 – 57711
    Beta strandi582 – 5876
    Turni588 – 5903
    Beta strandi591 – 60111

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3SL2X-ray1.61A451-611[»]
    ProteinModelPortaliQ45614.
    SMRiQ45614. Positions 203-255, 264-604.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1313CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini35 – 182148ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini204 – 611408CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei14 – 3421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei183 – 20321HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini204 – 25653HAMPPROSITE-ProRule annotationAdd
    BLAST
    Domaini263 – 32462PASAdd
    BLAST
    Domaini325 – 37955PACPROSITE-ProRule annotationAdd
    BLAST
    Domaini383 – 602220Histidine kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 HAMP domain.PROSITE-ProRule annotation
    Contains 1 histidine kinase domain.PROSITE-ProRule annotation
    Contains 1 PAC (PAS-associated C-terminal) domain.PROSITE-ProRule annotation
    Contains 1 PAS (PER-ARNT-SIM) domain.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5002.
    HOGENOMiHOG000223176.
    KOiK07652.
    OMAiMQVIDNI.
    OrthoDBiEOG6G4VQG.
    PhylomeDBiQ45614.

    Family and domain databases

    Gene3Di1.10.287.130. 1 hit.
    3.30.565.10. 1 hit.
    InterProiIPR003661. EnvZ-like_dim/P.
    IPR003660. HAMP_linker_domain.
    IPR003594. HATPase_ATP-bd.
    IPR001610. PAC.
    IPR000014. PAS.
    IPR000700. PAS-assoc_C.
    IPR004358. Sig_transdc_His_kin-like_C.
    IPR005467. Sig_transdc_His_kinase_core.
    IPR009082. Sig_transdc_His_kinase_dimeric.
    [Graphical view]
    PfamiPF00672. HAMP. 1 hit.
    PF02518. HATPase_c. 1 hit.
    PF00512. HisKA. 1 hit.
    PF13426. PAS_9. 1 hit.
    [Graphical view]
    PRINTSiPR00344. BCTRLSENSOR.
    SMARTiSM00304. HAMP. 1 hit.
    SM00387. HATPase_c. 1 hit.
    SM00388. HisKA. 1 hit.
    SM00086. PAC. 1 hit.
    SM00091. PAS. 1 hit.
    [Graphical view]
    SUPFAMiSSF47384. SSF47384. 1 hit.
    SSF55785. SSF55785. 1 hit.
    SSF55874. SSF55874. 1 hit.
    PROSITEiPS50885. HAMP. 1 hit.
    PS50109. HIS_KIN. 1 hit.
    PS50113. PAC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q45614-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNKVGFFRSI QFKITLIYVL LIIIAMQIIG VYFVNQVEKS LISSYEQSLN    50
    QRIDNLSYYI EQEYKSDNDS TVIKDDVSRI LNDFTKSDEV REISFVDKSY 100
    EVVGSSKPYG EEVAGKQTTD LIFKRIFSTK QSYLRKYYDP KSKIRVLISA 150
    KPVMTENQEV VGAIYVVASM EDVFNQMKTI NTILASGTGL ALVLTALLGI 200
    FLARTITHPL SDMRKQAMEL AKGNFSRKVK KYGHDEIGQL ATTFNHLTRE 250
    LEDAQAMTEG ERRKLASVIA YMTDGVIATN RNGAIILLNS PALELLNVSR 300
    ETALEMPITS LLGLQENYTF EDLVEQQDSM LLEIERDDEL TVLRVNFSVI 350
    QREHGKIDGL IAVIYDVTEQ EKMDQERREF VANVSHELRT PLTTMRSYLE 400
    ALAEGAWENK DIAPRFLMVT QNETERMIRL VNDLLQLSKF DSKDYQFNRE 450
    WIQIVRFMSL IIDRFEMTKE QHVEFIRNLP DRDLYVEIDQ DKITQVLDNI 500
    ISNALKYSPE GGHVTFSIDV NEEEELLYIS VKDEGIGIPK KDVEKVFDRF 550
    YRVDKARTRK LGGTGLGLAI AKEMVQAHGG DIWADSIEGK GTTITFTLPY 600
    KEEQEDDWDE A 611
    Length:611
    Mass (Da):70,034
    Last modified:November 1, 1996 - v1
    Checksum:i2E7B7CB538410AE7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D78193 Genomic DNA. Translation: BAA11299.1.
    AL009126 Genomic DNA. Translation: CAB16077.1.
    PIRiF70089.
    RefSeqiNP_391920.1. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB16077; CAB16077; BSU40400.
    GeneIDi937793.
    KEGGibsu:BSU40400.
    PATRICi18980158. VBIBacSub10457_4241.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D78193 Genomic DNA. Translation: BAA11299.1 .
    AL009126 Genomic DNA. Translation: CAB16077.1 .
    PIRi F70089.
    RefSeqi NP_391920.1. NC_000964.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3SL2 X-ray 1.61 A 451-611 [» ]
    ProteinModelPortali Q45614.
    SMRi Q45614. Positions 203-255, 264-604.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q45614. 2 interactions.
    STRINGi 224308.BSU40400.

    Chemistry

    ChEMBLi CHEMBL1075059.

    Proteomic databases

    PaxDbi Q45614.

    Protocols and materials databases

    DNASUi 937793.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB16077 ; CAB16077 ; BSU40400 .
    GeneIDi 937793.
    KEGGi bsu:BSU40400.
    PATRICi 18980158. VBIBacSub10457_4241.

    Organism-specific databases

    GenoListi BSU40400.

    Phylogenomic databases

    eggNOGi COG5002.
    HOGENOMi HOG000223176.
    KOi K07652.
    OMAi MQVIDNI.
    OrthoDBi EOG6G4VQG.
    PhylomeDBi Q45614.

    Enzyme and pathway databases

    BioCyci BSUB:BSU40400-MONOMER.
    BRENDAi 2.7.13.3. 700.

    Family and domain databases

    Gene3Di 1.10.287.130. 1 hit.
    3.30.565.10. 1 hit.
    InterProi IPR003661. EnvZ-like_dim/P.
    IPR003660. HAMP_linker_domain.
    IPR003594. HATPase_ATP-bd.
    IPR001610. PAC.
    IPR000014. PAS.
    IPR000700. PAS-assoc_C.
    IPR004358. Sig_transdc_His_kin-like_C.
    IPR005467. Sig_transdc_His_kinase_core.
    IPR009082. Sig_transdc_His_kinase_dimeric.
    [Graphical view ]
    Pfami PF00672. HAMP. 1 hit.
    PF02518. HATPase_c. 1 hit.
    PF00512. HisKA. 1 hit.
    PF13426. PAS_9. 1 hit.
    [Graphical view ]
    PRINTSi PR00344. BCTRLSENSOR.
    SMARTi SM00304. HAMP. 1 hit.
    SM00387. HATPase_c. 1 hit.
    SM00388. HisKA. 1 hit.
    SM00086. PAC. 1 hit.
    SM00091. PAS. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47384. SSF47384. 1 hit.
    SSF55785. SSF55785. 1 hit.
    SSF55874. SSF55874. 1 hit.
    PROSITEi PS50885. HAMP. 1 hit.
    PS50109. HIS_KIN. 1 hit.
    PS50113. PAC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence analysis of the 36-kb region between gntZ and trnY genes of Bacillus subtilis genome."
      Kasahara Y., Nakai S., Ogasawara N.
      DNA Res. 4:155-159(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168.
    2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
      Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
      , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
      Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.
    3. "A two-component signal transduction system essential for growth of Bacillus subtilis: implications for anti-infective therapy."
      Fabret C., Hoch J.A.
      J. Bacteriol. 180:6375-6383(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
      Strain: 168 / JH642.
    4. "The essential two-component regulatory system encoded by yycF and yycG modulates expression of the ftsAZ operon in Bacillus subtilis."
      Fukuchi K., Kasahara Y., Asai K., Kobayashi K., Moriya S., Ogasawara N.
      Microbiology 146:1573-1583(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
      Strain: 168.
    5. "Antibacterial agents that inhibit histidine protein kinase YycG of Bacillus subtilis."
      Yamamoto K., Kitayama T., Minagawa S., Watanabe T., Sawada S., Okamoto T., Utsumi R.
      Biosci. Biotechnol. Biochem. 65:2306-2310(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF HIS-386, INHIBITION BY IMIDAZOLE AND ZERUMBONE DERIVATIVES.
    6. "Genes controlled by the essential YycG/YycF two-component system of Bacillus subtilis revealed through a novel hybrid regulator approach."
      Howell A., Dubrac S., Andersen K.K., Noone D., Fert J., Msadek T., Devine K.
      Mol. Microbiol. 49:1639-1655(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: STUDY OF THE YYCF/YYCG REGULON.
    7. "YycH and YycI interact to regulate the essential YycFG two-component system in Bacillus subtilis."
      Szurmant H., Mohan M.A., Imus P.M., Hoch J.A.
      J. Bacteriol. 189:3280-3289(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH YYCH AND YYCI, SUBUNIT.
    8. "The essential YycFG two-component system controls cell wall metabolism in Bacillus subtilis."
      Bisicchia P., Noone D., Lioliou E., Howell A., Quigley S., Jensen T., Jarmer H., Devine K.M.
      Mol. Microbiol. 65:180-200(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiYYCG_BACSU
    AccessioniPrimary (citable) accession number: Q45614
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 19, 2002
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 125 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The imidazole derivatives NH125, NH126 and NH127 inhibited the incorporation of phosphate from ATP at 50 µg/ml. The zerumbone derivative NH0891 inhibited YycG.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3