ROK_BACSU
ID ROK_BACSU Reviewed; 191 AA.
AC O34857;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Repressor Rok;
GN Name=rok {ECO:0000303|PubMed:11849533}; Synonyms=ykuW;
GN OrderedLocusNames=BSU14240;
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;
RA Scanlan E., Devine K.M.;
RT "Sequence of the Bacillus subtilis chromosome from ykuA to cse-15.";
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
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, GENE NAME, INDUCTION, DISRUPTION PHENOTYPE, AND DNA-BINDING.
RC STRAIN=BD630;
RX PubMed=11849533; DOI=10.1046/j.1365-2958.2002.02727.x;
RA Hoa T.T., Tortosa P., Albano M., Dubnau D.;
RT "Rok (YkuW) regulates genetic competence in Bacillus subtilis by directly
RT repressing comK.";
RL Mol. Microbiol. 43:15-26(2002).
RN [4]
RP FUNCTION, DNA-BINDING, AND REGULON.
RC STRAIN=168;
RX PubMed=15743949; DOI=10.1128/jb.187.6.2010-2019.2005;
RA Albano M., Smits W.K., Ho L.T., Kraigher B., Mandic-Mulec I., Kuipers O.P.,
RA Dubnau D.;
RT "The Rok protein of Bacillus subtilis represses genes for cell surface and
RT extracellular functions.";
RL J. Bacteriol. 187:2010-2019(2005).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, DOMAIN, DISRUPTION PHENOTYPE,
RP AND DNA-BINDING.
RC STRAIN=168, and 168 / JH642;
RX PubMed=21085634; DOI=10.1371/journal.pgen.1001207;
RA Smits W.K., Grossman A.D.;
RT "The transcriptional regulator Rok binds A+T-rich DNA and is involved in
RT repression of a mobile genetic element in Bacillus subtilis.";
RL PLoS Genet. 6:E1001207-E1001207(2010).
CC -!- FUNCTION: Repressor of comK, the master regulator of competence
CC development (PubMed:11849533). Overexpression seems to be lethal
CC (PubMed:11849533). Represses at least 20 genes that specify membrane-
CC localized and secreted proteins, including some that encode products
CC with antibiotic activity (PubMed:15743949). Binds to many AT-rich sites
CC in the chromosome, many of which are known or thought to derive from
CC horizontal gene transfer; helps keep mobile element ICEBs1 quiescent in
CC the genome (PubMed:21085634). Binds to its own promoter and is thus
CC probably autoregulatory (PubMed:21085634).
CC {ECO:0000269|PubMed:11849533, ECO:0000269|PubMed:15743949,
CC ECO:0000269|PubMed:21085634}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid
CC {ECO:0000269|PubMed:21085634}. Note=Not uniformly distributed in the
CC nucleoid, it forms several clusters (PubMed:21085634).
CC {ECO:0000269|PubMed:21085634}.
CC -!- INDUCTION: Expression is constant during late log phase and for at
CC least 2 hours in stationary phase (at protein level) (PubMed:11849533).
CC Probably repressed by AbrB and SinR, as well as partially by ComK
CC (PubMed:11849533). Probably negatively regulates its own expression
CC (PubMed:11849533, PubMed:21085634). There are 1000-3000
CC proteins/chromosome in exponential phase grown in minimal medium
CC (PubMed:21085634). {ECO:0000269|PubMed:11849533,
CC ECO:0000269|PubMed:21085634, ECO:0000305|PubMed:21085634}.
CC -!- DOMAIN: The C-terminus (residues 95-191) binds DNA (PubMed:21085634).
CC {ECO:0000269|PubMed:21085634}.
CC -!- DISRUPTION PHENOTYPE: Increased expression of comK, increases
CC transformation about 5-fold, decreases sporulation efficiency about 5-
CC fold (PubMed:11849533). Increased excision of mobile element ICEBs1
CC (PubMed:21085634). {ECO:0000269|PubMed:11849533,
CC ECO:0000269|PubMed:21085634}.
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DR EMBL; AJ222587; CAA10886.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13297.1; -; Genomic_DNA.
DR PIR; D69867; D69867.
DR RefSeq; NP_389307.1; NC_000964.3.
DR RefSeq; WP_003232378.1; NZ_JNCM01000035.1.
DR PDB; 5ZUX; NMR; -; A=102-187.
DR PDB; 5ZUZ; NMR; -; A=97-191.
DR PDBsum; 5ZUX; -.
DR PDBsum; 5ZUZ; -.
DR AlphaFoldDB; O34857; -.
DR BMRB; O34857; -.
DR SMR; O34857; -.
DR STRING; 224308.BSU14240; -.
DR jPOST; O34857; -.
DR PaxDb; O34857; -.
DR PRIDE; O34857; -.
DR EnsemblBacteria; CAB13297; CAB13297; BSU_14240.
DR GeneID; 938793; -.
DR KEGG; bsu:BSU14240; -.
DR PATRIC; fig|224308.179.peg.1554; -.
DR eggNOG; ENOG502ZXGY; Bacteria.
DR OMA; PQMQSIT; -.
DR BioCyc; BSUB:BSU14240-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0009295; C:nucleoid; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Cytoplasm; DNA-binding; Reference proteome;
KW Repressor; Transcription; Transcription regulation.
FT CHAIN 1..191
FT /note="Repressor Rok"
FT /id="PRO_0000097399"
FT REGION 75..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..191
FT /note="DNA-binding"
FT /evidence="ECO:0000269|PubMed:21085634"
FT COILED 2..43
FT /evidence="ECO:0000255"
FT COMPBIAS 75..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:5ZUZ"
FT HELIX 118..129
FT /evidence="ECO:0007829|PDB:5ZUX"
FT HELIX 137..148
FT /evidence="ECO:0007829|PDB:5ZUX"
FT HELIX 155..165
FT /evidence="ECO:0007829|PDB:5ZUX"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:5ZUX"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:5ZUX"
FT HELIX 183..186
FT /evidence="ECO:0007829|PDB:5ZUX"
SQ SEQUENCE 191 AA; 21840 MW; 83AAF7DECDD7232A CRC64;
MFNEREALRL RLEQLNEAEV KVIREYQIER DKIYAKLREL DRNGSPSEIK KDFRSEKKPD
SLPVLAELAA QEIRSYQPQS QQQSVQPQLQ SISSLPAGIP DGTTRRRRGT ARPGSKAAKL
REAAIKTLKR HNAAIKSSEL QKEIEKESGL EIPNMTTFMQ SLIKMYPEVK KPYRGQYILE
GEIESAESAN E
