ID YYCH_BACSU Reviewed; 455 AA.
AC Q794W0; Q45613;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE RecName: Full=Two-component system WalR/WalK regulatory protein YycH;
GN Name=yycH; OrderedLocusNames=BSU40390;
OS Bacillus subtilis (strain 168).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9205843; DOI=10.1093/dnares/4.2.155;
RA Kasahara Y., Nakai S., Ogasawara N.;
RT "Sequence analysis of the 36-kb region between gntZ and trnY genes of
RT Bacillus subtilis genome.";
RL DNA Res. 4:155-159(1997).
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 REGULATION OF WALR/WALK, AND DISRUPTION PHENOTYPE.
RX PubMed=16030236; DOI=10.1128/jb.187.15.5419-5426.2005;
RA Szurmant H., Nelson K., Kim E.-J., Perego M., Hoch J.A.;
RT "YycH regulates the activity of the essential YycFG two-component system in
RT Bacillus subtilis.";
RL J. Bacteriol. 187:5419-5426(2005).
RN [4]
RP FUNCTION, TOPOLOGY, DISRUPTION PHENOTYPE, AND INTERACTION WITH WALK AND
RP YYCI.
RX PubMed=17307850; DOI=10.1128/jb.01936-06;
RA Szurmant H., Mohan M.A., Imus P.M., Hoch J.A.;
RT "YycH and YycI interact to regulate the essential YycFG two-component
RT system in Bacillus subtilis.";
RL J. Bacteriol. 189:3280-3289(2007).
RN [5]
RP FUNCTION, MUTAGENESIS OF THR-22 AND TRP-26, AND DOMAIN.
RX PubMed=18408157; DOI=10.1073/pnas.0800247105;
RA Szurmant H., Bu L., Brooks C.L. III, Hoch J.A.;
RT "An essential sensor histidine kinase controlled by transmembrane helix
RT interactions with its auxiliary proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:5891-5896(2008).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 39-458 IN COMPLEX WITH CALCIUM
RP IONS.
RX PubMed=16600972; DOI=10.1110/ps.052064406;
RA Szurmant H., Zhao H., Mohan M.A., Hoch J.A., Varughese K.I.;
RT "The crystal structure of YycH involved in the regulation of the essential
RT YycFG two-component system in Bacillus subtilis reveals a novel tertiary
RT structure.";
RL Protein Sci. 15:929-934(2006).
CC -!- FUNCTION: Together with YycI, regulates the activity of the two-
CC component system WalR/WalK. {ECO:0000269|PubMed:17307850,
CC ECO:0000269|PubMed:18408157}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with WalK and YycI.
CC {ECO:0000250, ECO:0000269|PubMed:16600972,
CC ECO:0000269|PubMed:17307850}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- DOMAIN: The transmembrane region is required for the regulation of WalK
CC activity. {ECO:0000269|PubMed:18408157}.
CC -!- DISRUPTION PHENOTYPE: No cellular levels increase of either WalK or
CC WalR. Induction of WalR-dependent gene expression. Cell wall defect.
CC {ECO:0000269|PubMed:16030236, ECO:0000269|PubMed:17307850}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA11298.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D78193; BAA11298.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL009126; CAB16076.1; -; Genomic_DNA.
DR PIR; G70089; G70089.
DR RefSeq; NP_391919.1; NC_000964.3.
DR RefSeq; WP_003242498.1; NZ_JNCM01000034.1.
DR PDB; 2FGT; X-ray; 2.30 A; A=39-455.
DR PDBsum; 2FGT; -.
DR AlphaFoldDB; Q794W0; -.
DR SMR; Q794W0; -.
DR STRING; 224308.BSU40390; -.
DR PaxDb; 224308-BSU40390; -.
DR EnsemblBacteria; CAB16076; CAB16076; BSU_40390.
DR GeneID; 937790; -.
DR KEGG; bsu:BSU40390; -.
DR PATRIC; fig|224308.179.peg.4372; -.
DR eggNOG; COG4863; Bacteria.
DR InParanoid; Q794W0; -.
DR OrthoDB; 2382185at2; -.
DR PhylomeDB; Q794W0; -.
DR BioCyc; BSUB:BSU40390-MONOMER; -.
DR EvolutionaryTrace; Q794W0; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15785; YycH_N_like; 1.
DR Gene3D; 3.10.450.310; -; 1.
DR Gene3D; 3.30.310.160; YycH protein, domain 2; 1.
DR InterPro; IPR009996; YycH.
DR InterPro; IPR042274; YycH/YycI_2.
DR Pfam; PF07435; YycH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell membrane; Membrane; Metal-binding;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..455
FT /note="Two-component system WalR/WalK regulatory protein
FT YycH"
FT /id="PRO_0000066553"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..455
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT BINDING 69
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 70
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 115
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 117
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 119
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT MUTAGEN 22
FT /note="T->F: Slight induction of WalK-dependent genes."
FT /evidence="ECO:0000269|PubMed:18408157"
FT MUTAGEN 26
FT /note="W->A: Slight induction of WalK-dependent genes."
FT /evidence="ECO:0000269|PubMed:18408157"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:2FGT"
FT STRAND 63..69
FT /evidence="ECO:0007829|PDB:2FGT"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:2FGT"
FT HELIX 79..88
FT /evidence="ECO:0007829|PDB:2FGT"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:2FGT"
FT STRAND 92..99
FT /evidence="ECO:0007829|PDB:2FGT"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:2FGT"
FT HELIX 106..113
FT /evidence="ECO:0007829|PDB:2FGT"
FT STRAND 122..132
FT /evidence="ECO:0007829|PDB:2FGT"
FT HELIX 133..140
FT /evidence="ECO:0007829|PDB:2FGT"
FT STRAND 151..159
FT /evidence="ECO:0007829|PDB:2FGT"
FT STRAND 163..172
FT /evidence="ECO:0007829|PDB:2FGT"
FT TURN 173..176
FT /evidence="ECO:0007829|PDB:2FGT"
FT STRAND 177..184
FT /evidence="ECO:0007829|PDB:2FGT"
FT HELIX 188..198
FT /evidence="ECO:0007829|PDB:2FGT"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:2FGT"
FT STRAND 204..210
FT /evidence="ECO:0007829|PDB:2FGT"
FT TURN 211..213
FT /evidence="ECO:0007829|PDB:2FGT"
FT STRAND 214..221
FT /evidence="ECO:0007829|PDB:2FGT"
FT STRAND 223..226
FT /evidence="ECO:0007829|PDB:2FGT"
FT HELIX 237..244
FT /evidence="ECO:0007829|PDB:2FGT"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:2FGT"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:2FGT"
FT STRAND 269..273
FT /evidence="ECO:0007829|PDB:2FGT"
FT TURN 274..277
FT /evidence="ECO:0007829|PDB:2FGT"
FT STRAND 278..282
FT /evidence="ECO:0007829|PDB:2FGT"
FT HELIX 294..307
FT /evidence="ECO:0007829|PDB:2FGT"
FT STRAND 315..320
FT /evidence="ECO:0007829|PDB:2FGT"
FT STRAND 326..332
FT /evidence="ECO:0007829|PDB:2FGT"
FT STRAND 335..339
FT /evidence="ECO:0007829|PDB:2FGT"
FT STRAND 341..343
FT /evidence="ECO:0007829|PDB:2FGT"
FT STRAND 350..355
FT /evidence="ECO:0007829|PDB:2FGT"
FT STRAND 357..367
FT /evidence="ECO:0007829|PDB:2FGT"
FT STRAND 379..382
FT /evidence="ECO:0007829|PDB:2FGT"
FT HELIX 386..393
FT /evidence="ECO:0007829|PDB:2FGT"
FT HELIX 400..402
FT /evidence="ECO:0007829|PDB:2FGT"
FT STRAND 403..412
FT /evidence="ECO:0007829|PDB:2FGT"
FT STRAND 426..433
FT /evidence="ECO:0007829|PDB:2FGT"
FT STRAND 436..441
FT /evidence="ECO:0007829|PDB:2FGT"
SQ SEQUENCE 455 AA; 52215 MW; D3A9FD9CE22CFE83 CRC64;
MKRENIKTIL LTVLVVISLV FTWGIWTFQP NFSEGSSSTE STVRVKHKIE KTTQKLSETV
RPRDMFIHDD GAHYKVDDNA LYEEIWSDLP HWDVKGIKDI SDQYDKAGFK SWFYGIGGSE
AKLDLQFSDT IPIDIFQTLF KWSNQSFEYS SFDHILIPFN ETKANKKIYL VSYSKQLILE
VTVESANYRN IMNDLKNRQS NMPAFSLFSI GSKKEFLLPN KPLTMDKKEF VTESIKTNTF
KQALFSDPSI VREDSNYNNR NVLTDGISRL DVNLSQRQVQ FQQRNLVQST SYQTGELIKK
SQKYLEDTGS WTDHYQFFNI NDSQQLSFYI FMDQIPVINS TAKPFGATSA ITVQWANDDI
LSYKRPNYSL GTNPIKTSET ELMGGSEVKM LLSKQTAYDT DKIDQIFLAY QLVSTSTNDD
PLVELEPVWA MKVNGKIVPI TKDLLRKEGA NSGVE
//
