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Protein

Sensor histidine kinase YycG

Gene

yycG

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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
Complete GO annotation...

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. 658.

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 Componenti: Chromosome

Organism-specific databases

GenoListiBSU40400.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1313CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei14 – 3421HelicalSequence AnalysisAdd
BLAST
Topological domaini35 – 182148ExtracellularSequence AnalysisAdd
BLAST
Transmembranei183 – 20321HelicalSequence AnalysisAdd
BLAST
Topological domaini204 – 611408CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

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

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 – 4533Combined sources
Helixi454 – 46613Combined sources
Beta strandi475 – 4784Combined sources
Beta strandi485 – 4884Combined sources
Helixi490 – 50617Combined sources
Beta strandi514 – 5218Combined sources
Turni522 – 5254Combined sources
Beta strandi526 – 5327Combined sources
Turni540 – 5478Combined sources
Helixi567 – 57711Combined sources
Beta strandi582 – 5876Combined sources
Turni588 – 5903Combined sources
Beta strandi591 – 60111Combined sources

3D structure databases

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

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.
InParanoidiQ45614.
KOiK07652.
OMAiLTTMKSY.
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_C.
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

        10         20         30         40         50
MNKVGFFRSI QFKITLIYVL LIIIAMQIIG VYFVNQVEKS LISSYEQSLN
60 70 80 90 100
QRIDNLSYYI EQEYKSDNDS TVIKDDVSRI LNDFTKSDEV REISFVDKSY
110 120 130 140 150
EVVGSSKPYG EEVAGKQTTD LIFKRIFSTK QSYLRKYYDP KSKIRVLISA
160 170 180 190 200
KPVMTENQEV VGAIYVVASM EDVFNQMKTI NTILASGTGL ALVLTALLGI
210 220 230 240 250
FLARTITHPL SDMRKQAMEL AKGNFSRKVK KYGHDEIGQL ATTFNHLTRE
260 270 280 290 300
LEDAQAMTEG ERRKLASVIA YMTDGVIATN RNGAIILLNS PALELLNVSR
310 320 330 340 350
ETALEMPITS LLGLQENYTF EDLVEQQDSM LLEIERDDEL TVLRVNFSVI
360 370 380 390 400
QREHGKIDGL IAVIYDVTEQ EKMDQERREF VANVSHELRT PLTTMRSYLE
410 420 430 440 450
ALAEGAWENK DIAPRFLMVT QNETERMIRL VNDLLQLSKF DSKDYQFNRE
460 470 480 490 500
WIQIVRFMSL IIDRFEMTKE QHVEFIRNLP DRDLYVEIDQ DKITQVLDNI
510 520 530 540 550
ISNALKYSPE GGHVTFSIDV NEEEELLYIS VKDEGIGIPK KDVEKVFDRF
560 570 580 590 600
YRVDKARTRK LGGTGLGLAI AKEMVQAHGG DIWADSIEGK GTTITFTLPY
610
KEEQEDDWDE A
Length:611
Mass (Da):70,034
Last modified:November 1, 1996 - v1
Checksum:i2E7B7CB538410AE7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
D78193 Genomic DNA. Translation: BAA11299.1.
AL009126 Genomic DNA. Translation: CAB16077.1.
PIRiF70089.
RefSeqiNP_391920.1. NC_000964.3.

3D structure databases

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

Protein-protein interaction databases

IntActiQ45614. 2 interactions.
STRINGi224308.BSU40400.

Chemistry

BindingDBiQ45614.
ChEMBLiCHEMBL1075059.

Proteomic databases

PaxDbiQ45614.

Protocols and materials databases

DNASUi937793.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

GenoListiBSU40400.

Phylogenomic databases

eggNOGiCOG5002.
HOGENOMiHOG000223176.
InParanoidiQ45614.
KOiK07652.
OMAiLTTMKSY.
OrthoDBiEOG6G4VQG.
PhylomeDBiQ45614.

Enzyme and pathway databases

BioCyciBSUB:BSU40400-MONOMER.
BRENDAi2.7.13.3. 658.

Miscellaneous databases

PROiQ45614.

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_C.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: April 29, 2015
This is version 130 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.