YYCI_BACSU
ID YYCI_BACSU Reviewed; 280 AA.
AC Q45612; Q794W1;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Two-component system WalR/WalK regulatory protein YycI;
GN Name=yycI; OrderedLocusNames=BSU40380;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; 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 FUNCTION, TOPOLOGY, DISRUPTION PHENOTYPE, AND INTERACTION WITH WALK AND
RP YYCH.
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 [4]
RP FUNCTION, MUTAGENESIS OF PHE-10; PHE-14; ASP-18; LEU-21 AND PHE-25, AND
RP 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 [5]
RP X-RAY CRYSTALLOGRAPHY (2.89 ANGSTROMS) OF 31-280, AND SUBUNIT.
RX PubMed=17307848; DOI=10.1128/jb.01937-06;
RA Santelli E., Liddington R.C., Mohan M.A., Hoch J.A., Szurmant H.;
RT "The crystal structure of Bacillus subtilis YycI reveals a common fold for
RT two members of an unusual class of sensor histidine kinase regulatory
RT proteins.";
RL J. Bacteriol. 189:3290-3295(2007).
CC -!- FUNCTION: Together with YycH, regulates the activity of the two-
CC component system WalR/WalK. {ECO:0000269|PubMed:17307850,
CC ECO:0000269|PubMed:18408157}.
CC -!- SUBUNIT: Homodimer. Interacts with WalK and YycH.
CC {ECO:0000269|PubMed:17307848, 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: Induction of WalR-dependent gene expression. Cell
CC wall defect. {ECO:0000269|PubMed:17307850}.
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DR EMBL; D78193; BAA11297.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB16075.1; -; Genomic_DNA.
DR PIR; H70089; H70089.
DR RefSeq; NP_391918.1; NC_000964.3.
DR RefSeq; WP_003244037.1; NZ_JNCM01000034.1.
DR PDB; 2O3O; X-ray; 2.89 A; A/B/C/D/E/F/G/H/I/J/K/L=31-280.
DR PDBsum; 2O3O; -.
DR AlphaFoldDB; Q45612; -.
DR SMR; Q45612; -.
DR STRING; 224308.BSU40380; -.
DR PaxDb; Q45612; -.
DR PRIDE; Q45612; -.
DR EnsemblBacteria; CAB16075; CAB16075; BSU_40380.
DR GeneID; 937765; -.
DR KEGG; bsu:BSU40380; -.
DR PATRIC; fig|224308.179.peg.4371; -.
DR eggNOG; COG4853; Bacteria.
DR OMA; TWHIVVN; -.
DR PhylomeDB; Q45612; -.
DR BioCyc; BSUB:BSU40380-MON; -.
DR EvolutionaryTrace; Q45612; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR018604; YycI-like.
DR Pfam; PF09648; YycI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..280
FT /note="Two-component system WalR/WalK regulatory protein
FT YycI"
FT /id="PRO_0000360822"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..280
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT MUTAGEN 10
FT /note="F->A: Induction of WalK-dependent genes."
FT /evidence="ECO:0000269|PubMed:18408157"
FT MUTAGEN 14
FT /note="F->A: Induction of WalK-dependent genes."
FT /evidence="ECO:0000269|PubMed:18408157"
FT MUTAGEN 18
FT /note="D->A: Induction of WalK-dependent genes."
FT /evidence="ECO:0000269|PubMed:18408157"
FT MUTAGEN 21
FT /note="L->A: Induction of WalK-dependent genes."
FT /evidence="ECO:0000269|PubMed:18408157"
FT MUTAGEN 25
FT /note="F->A: Induction of WalK-dependent genes."
FT /evidence="ECO:0000269|PubMed:18408157"
FT HELIX 35..49
FT /evidence="ECO:0007829|PDB:2O3O"
FT STRAND 62..71
FT /evidence="ECO:0007829|PDB:2O3O"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:2O3O"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:2O3O"
FT STRAND 99..110
FT /evidence="ECO:0007829|PDB:2O3O"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:2O3O"
FT HELIX 116..127
FT /evidence="ECO:0007829|PDB:2O3O"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:2O3O"
FT STRAND 134..140
FT /evidence="ECO:0007829|PDB:2O3O"
FT TURN 141..144
FT /evidence="ECO:0007829|PDB:2O3O"
FT STRAND 145..152
FT /evidence="ECO:0007829|PDB:2O3O"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:2O3O"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:2O3O"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:2O3O"
FT STRAND 168..175
FT /evidence="ECO:0007829|PDB:2O3O"
FT STRAND 177..187
FT /evidence="ECO:0007829|PDB:2O3O"
FT STRAND 189..200
FT /evidence="ECO:0007829|PDB:2O3O"
FT HELIX 203..212
FT /evidence="ECO:0007829|PDB:2O3O"
FT STRAND 221..235
FT /evidence="ECO:0007829|PDB:2O3O"
FT STRAND 238..252
FT /evidence="ECO:0007829|PDB:2O3O"
FT STRAND 261..269
FT /evidence="ECO:0007829|PDB:2O3O"
FT STRAND 274..277
FT /evidence="ECO:0007829|PDB:2O3O"
SQ SEQUENCE 280 AA; 32594 MW; 991C958F77F58C77 CRC64;
MEWNKTKSIF IVAFLILDIF LGYQFFQKWQ ATGKEYEVIK NDVEHDMKAD HITYEGLNKE
ATEGYRITAN QKSFSKEEIE ALKDQKPLMD MPSDDHKVTS LKMKFANPIA LSKKDIEDDA
QALVSSKIQD GEKYKLWKVD KSKKEIIFFQ TYEGHYIYQK TDNPSNMIGQ VVLHLNGKNE
VVSYDQTTLE TFKQIQKESL ITEMDAVELL YYQNQLKEYS TVKSCKFGYV AQYPLTSTQV
LAPVWRITVE YEKKVNGEKK TVQEYFTVNA LESTILDTDQ