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Q45614 (YYCG_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sensor histidine kinase YycG
EC=2.7.13.3
Gene names
Name:yycG
Ordered Locus Names:BSU40400
OrganismBacillus subtilis
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length611 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.3 Ref.4 Ref.8

Catalytic activity

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

Subunit structure

Homodimer. Interacts with YycH and YycI. Ref.7

Subcellular location

Cell membrane; Multi-pass membrane protein Probable.

Developmental stage

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

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.

Sequence similarities

Contains 1 HAMP domain.

Contains 1 histidine kinase domain.

Contains 1 PAC (PAS-associated C-terminal) domain.

Contains 1 PAS (PER-ARNT-SIM) domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 611611Sensor histidine kinase YycG
PRO_0000074918

Regions

Topological domain1 – 1313Cytoplasmic Potential
Transmembrane14 – 3421Helical; Potential
Topological domain35 – 182148Extracellular Potential
Transmembrane183 – 20321Helical; Potential
Topological domain204 – 611408Cytoplasmic Potential
Domain204 – 25653HAMP
Domain263 – 32462PAS
Domain325 – 37955PAC
Domain383 – 602220Histidine kinase

Amino acid modifications

Modified residue3861Phosphohistidine; by autocatalysis Probable

Experimental info

Mutagenesis3861H → R or A: Loss of phosphorylation. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q45614 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 2E7B7CB538410AE7

FASTA61170,034
        10         20         30         40         50         60 
MNKVGFFRSI QFKITLIYVL LIIIAMQIIG VYFVNQVEKS LISSYEQSLN QRIDNLSYYI 

        70         80         90        100        110        120 
EQEYKSDNDS TVIKDDVSRI LNDFTKSDEV REISFVDKSY EVVGSSKPYG EEVAGKQTTD 

       130        140        150        160        170        180 
LIFKRIFSTK QSYLRKYYDP KSKIRVLISA KPVMTENQEV VGAIYVVASM EDVFNQMKTI 

       190        200        210        220        230        240 
NTILASGTGL ALVLTALLGI FLARTITHPL SDMRKQAMEL AKGNFSRKVK KYGHDEIGQL 

       250        260        270        280        290        300 
ATTFNHLTRE LEDAQAMTEG ERRKLASVIA YMTDGVIATN RNGAIILLNS PALELLNVSR 

       310        320        330        340        350        360 
ETALEMPITS LLGLQENYTF EDLVEQQDSM LLEIERDDEL TVLRVNFSVI QREHGKIDGL 

       370        380        390        400        410        420 
IAVIYDVTEQ EKMDQERREF VANVSHELRT PLTTMRSYLE ALAEGAWENK DIAPRFLMVT 

       430        440        450        460        470        480 
QNETERMIRL VNDLLQLSKF DSKDYQFNRE WIQIVRFMSL IIDRFEMTKE QHVEFIRNLP 

       490        500        510        520        530        540 
DRDLYVEIDQ DKITQVLDNI ISNALKYSPE GGHVTFSIDV NEEEELLYIS VKDEGIGIPK 

       550        560        570        580        590        600 
KDVEKVFDRF YRVDKARTRK LGGTGLGLAI AKEMVQAHGG DIWADSIEGK GTTITFTLPY 

       610 
KEEQEDDWDE A

« Hide

References

« Hide 'large scale' references
[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: 9205843] [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. expand/collapse author list , 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: 9384377] [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: 9829949] [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: 10878122] [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: 11758928] [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: 12950927] [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: 17307850] [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: 17581128] [Abstract]
Cited for: FUNCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D78193 Genomic DNA. Translation: BAA11299.1.
AL009126 Genomic DNA. Translation: CAB16077.1.
PIRF70089.
RefSeqNP_391920.1. NC_000964.3.

3D structure databases

ProteinModelPortalQ45614.
SMRQ45614. Positions 203-255, 264-604.
ModBaseSearch...

Protein-protein interaction databases

IntActQ45614. 4 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000002363; EBBACP00000002363; EBBACG00000002358.
GeneID937793.
GenomeReviewsGene locus BSU40400 in contig AL009126_GR.
KEGGbsu:BSU40400.
NMPDRfig|224308.1.peg.4046.
PATRIC18980158. VBIBacSub10457_4241.

Organism-specific databases

GenoListBSU40400.

Phylogenomic databases

GeneTreeEBGT00070000031815.
HOGENOMHBG334875.
OMAAMQIIGV.
PhylomeDBQ45614.
ProtClustDBCLSK888192.

Enzyme and pathway databases

BioCycBSUB:BSU40400-MONOMER.
BRENDA2.7.13.3. 700.

Family and domain databases

InterProIPR003594. ATPase-like_ATP-bd.
IPR003660. HAMP_linker_domain.
IPR001610. PAC.
IPR000014. PAS.
IPR000700. PAS-assoc_C.
IPR004358. Sig_transdc_His_kin-like_C.
IPR003661. Sig_transdc_His_kin_sub1_dim/P.
IPR005467. Sig_transdc_His_kinase_core.
IPR009082. Sig_transdc_His_kinase_dimeric.
[Graphical view]
Gene3DG3DSA:3.30.565.10. ATP_bd_ATPase. 1 hit.
KOK07652.
PfamPF00672. HAMP. 1 hit.
PF02518. HATPase_c. 1 hit.
PF00512. HisKA. 1 hit.
[Graphical view]
PRINTSPR00344. BCTRLSENSOR.
SMARTSM00304. HAMP. 1 hit.
SM00387. HATPase_c. 1 hit.
SM00388. HisKA. 1 hit.
SM00086. PAC. 1 hit.
SM00091. PAS. 1 hit.
[Graphical view]
SUPFAMSSF55874. ATP_bd_ATPase. 1 hit.
SSF47384. His_kin_homodim. 1 hit.
PROSITEPS50885. HAMP. 1 hit.
PS50109. HIS_KIN. 1 hit.
PS50113. PAC. 1 hit.
PS50112. PAS. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameYYCG_BACSU
AccessionPrimary (citable) accession number: Q45614
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: November 1, 1996
Last modified: January 25, 2012
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents