Q45614 (YYCG_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Sensor histidine kinase YycG
EC=2.7.13.3

Gene names

Name:	yycG
Ordered Locus Names:	BSU40400

Organism

Bacillus subtilis (strain 168) [Reference proteome] [HAMAP]

Taxonomic identifier

224308 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus subtilis group › Bacillus subtilis › Bacillus subtilis subsp. subtilis

Protein attributes

Sequence length	611 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Two-component regulatory system
Cellular component	Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro signal transduction by phosphorylation Inferred from electronic annotation. Source: GOC
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW phosphorelay sensor kinase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 611

611

Sensor histidine kinase YycG

PRO_0000074918

Regions

Topological domain

1 – 13

13

Cytoplasmic Potential

Transmembrane

14 – 34

21

Helical; Potential

Topological domain

35 – 182

148

Extracellular Potential

Transmembrane

183 – 203

21

Helical; Potential

Topological domain

204 – 611

408

Cytoplasmic Potential

Domain

204 – 256

53

HAMP

Domain

263 – 324

62

PAS

Domain

325 – 379

55

PAC

Domain

383 – 602

220

Histidine kinase

Amino acid modifications

Modified residue

386

1

Phosphohistidine; by autocatalysis Probable

Experimental info

Mutagenesis

386

1

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

Secondary structure

1

.

.

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.

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611

Helix Strand Turn

Details...

Beta strand

451 – 453

3

Helix

454 – 466

13

Beta strand

475 – 478

4

Beta strand

485 – 488

4

Helix

490 – 506

17

Beta strand

514 – 521

8

Turn

522 – 525

4

Beta strand

526 – 532

7

Turn

540 – 547

8

Helix

567 – 577

11

Beta strand

582 – 587

6

Turn

588 – 590

3

Beta strand

591 – 601

11

Sequences

	Sequence		Length	Mass (Da)
	Q45614 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 2E7B7CB538410AE7	FASTA	611	70,034
	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

References

	« Hide 'large scale' referencesShow '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] [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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D78193 Genomic DNA. Translation: BAA11299.1.
AL009126 Genomic DNA. Translation: CAB16077.1.

PIR

F70089.

RefSeq

NP_391920.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3SL2	X-ray	1.61	A	451-611	[»]

ProteinModelPortal

Q45614.

SMR

Q45614. Positions 203-255, 264-604.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q45614. 2 interactions.

STRING

224308.BSU40400.

Proteomic databases

PaxDb

Q45614.

Protocols and materials databases

DNASU

937793.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

CAB16077; CAB16077; BSU40400.

GeneID

937793.

KEGG

bsu:BSU40400.

PATRIC

18980158. VBIBacSub10457_4241.

Organism-specific databases

GenoList

BSU40400.

Phylogenomic databases

eggNOG

COG5002.

HOGENOM

HOG000223176.

KO

K07652.

OMA

AMQIIGV.

ProtClustDB

CLSK888192.

Enzyme and pathway databases

BioCyc

BSUB:BSU40400-MONOMER.

BRENDA

2.7.13.3. 700.

Family and domain databases

Gene3D

1.10.287.130. 1 hit.
3.30.565.10. 1 hit.

InterPro

IPR003660. HAMP_linker_domain.
IPR003594. HATPase_ATP-bd.
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]

Pfam

PF00672. HAMP. 1 hit.
PF02518. HATPase_c. 1 hit.
PF00512. HisKA. 1 hit.
[Graphical view]

PRINTS

PR00344. BCTRLSENSOR.

SMART

SM00304. HAMP. 1 hit.
SM00387. HATPase_c. 1 hit.
SM00388. HisKA. 1 hit.
SM00086. PAC. 1 hit.
SM00091. PAS. 1 hit.
[Graphical view]

SUPFAM

SSF55874. ATP_bd_ATPase. 1 hit.
SSF47384. His_kin_homodim. 1 hit.

PROSITE

PS50885. HAMP. 1 hit.
PS50109. HIS_KIN. 1 hit.
PS50113. PAC. 1 hit.
PS50112. PAS. False negative.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL1075059.

Entry information

Entry name

YYCG_BACSU

Accession

Primary (citable) accession number: Q45614

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2002
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 115 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program