CYMR_BACSU
ID CYMR_BACSU Reviewed; 138 AA.
AC O34527;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=HTH-type transcriptional regulator CymR;
DE AltName: Full=Cysteine metabolism repressor;
GN Name=cymR; Synonyms=yrzC; OrderedLocusNames=BSU27520;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
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 [2]
RP SEQUENCE REVISION TO C-TERMINUS.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [3]
RP FUNCTION AS A CYSTEINE METABOLISM REPRESSOR, REGULATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=168;
RX PubMed=16513748; DOI=10.1128/jb.188.6.2184-2197.2006;
RA Even S., Burguiere P., Auger S., Soutourina O., Danchin A.,
RA Martin-Verstraete I.;
RT "Global control of cysteine metabolism by CymR in Bacillus subtilis.";
RL J. Bacteriol. 188:2184-2197(2006).
RN [4]
RP FUNCTION, REGULATION, SUBUNIT, AND INTERACTION WITH CYSK.
RC STRAIN=168;
RX PubMed=18974048; DOI=10.1074/jbc.m805951200;
RA Tanous C., Soutourina O., Raynal B., Hullo M.-F., Mervelet P.,
RA Gilles A.-M., Noirot P., Danchin A., England P., Martin-Verstraete I.;
RT "The CymR regulator in complex with the enzyme CysK controls cysteine
RT metabolism in Bacillus subtilis.";
RL J. Biol. Chem. 283:35551-35560(2008).
CC -!- FUNCTION: Master repressor of cysteine metabolism in B.subtilis.
CC Controls the expression of genes involved either in cysteine synthesis
CC from sulfide (cysK), sulfonates (ssu), or methionine (mccAB) or in
CC cystine uptake (tcyP). Activity of CymR is positively regulated by CysK
CC in response to cysteine availability. When cysteine is present, the
CC pool of O-acetylserine (OAS) is low, which leads to the formation of a
CC CymR-CysK complex and transcriptional repression of the CymR regulon
CC occurs. In the absence of cysteine, the OAS pool is high and the CymR-
CC CysK complex is mostly dissociated, leading to a faster dissociation of
CC CymR from its DNA targets and the lifting of CymR-dependent repression.
CC {ECO:0000269|PubMed:16513748, ECO:0000269|PubMed:18974048}.
CC -!- SUBUNIT: Homodimer. Forms homotetramers at higher concentrations of
CC protein. Forms CymR(2):CysK(2) or CymR(4):CysK(4) complexes in the
CC absence of O-acetylserine. {ECO:0000269|PubMed:18974048}.
CC -!- INTERACTION:
CC O34527; O34527: cymR; NbExp=2; IntAct=EBI-6964678, EBI-6964678;
CC -!- DISRUPTION PHENOTYPE: Grows slowly with cystine as sole sulfur source.
CC {ECO:0000269|PubMed:16513748}.
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DR EMBL; AL009126; CAB14694.2; -; Genomic_DNA.
DR PIR; B69982; B69982.
DR RefSeq; NP_390630.2; NC_000964.3.
DR RefSeq; WP_003225879.1; NZ_JNCM01000036.1.
DR PDB; 2Y75; X-ray; 2.00 A; A/B/C/D/E/F=1-128.
DR PDBsum; 2Y75; -.
DR AlphaFoldDB; O34527; -.
DR SMR; O34527; -.
DR MINT; O34527; -.
DR STRING; 224308.BSU27520; -.
DR EnsemblBacteria; CAB14694; CAB14694; BSU_27520.
DR GeneID; 50136793; -.
DR GeneID; 64304472; -.
DR GeneID; 936456; -.
DR KEGG; bsu:BSU27520; -.
DR PATRIC; fig|224308.179.peg.2990; -.
DR eggNOG; COG1959; Bacteria.
DR InParanoid; O34527; -.
DR OMA; YGLTIMM; -.
DR PhylomeDB; O34527; -.
DR BioCyc; BSUB:BSU27520-MON; -.
DR EvolutionaryTrace; O34527; -.
DR PRO; PR:O34527; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IDA:CAFA.
DR GO; GO:0032993; C:protein-DNA complex; IDA:CAFA.
DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; IDA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:CAFA.
DR GO; GO:0051291; P:protein heterooligomerization; IDA:CAFA.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR030489; TR_Rrf2-type_CS.
DR InterPro; IPR000944; Tscrpt_reg_Rrf2.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR33221; PTHR33221; 1.
DR Pfam; PF02082; Rrf2; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR TIGRFAMs; TIGR00738; rrf2_super; 1.
DR PROSITE; PS01332; HTH_RRF2_1; 1.
DR PROSITE; PS51197; HTH_RRF2_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..138
FT /note="HTH-type transcriptional regulator CymR"
FT /id="PRO_0000109568"
FT DOMAIN 2..125
FT /note="HTH rrf2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00540"
FT DNA_BIND 28..51
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00540"
FT HELIX 5..19
FT /evidence="ECO:0007829|PDB:2Y75"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:2Y75"
FT HELIX 28..34
FT /evidence="ECO:0007829|PDB:2Y75"
FT HELIX 39..51
FT /evidence="ECO:0007829|PDB:2Y75"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:2Y75"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:2Y75"
FT HELIX 76..84
FT /evidence="ECO:0007829|PDB:2Y75"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:2Y75"
FT HELIX 98..117
FT /evidence="ECO:0007829|PDB:2Y75"
FT HELIX 120..124
FT /evidence="ECO:0007829|PDB:2Y75"
SQ SEQUENCE 138 AA; 15255 MW; A469EA0E4133C351 CRC64;
MKISTKGRYG LTIMIELAKK HGEGPTSLKS IAQTNNLSEH YLEQLVSPLR NAGLVKSIRG
AYGGYVLGSE PDAITAGDII RVLEGPISPV EVLEDEEPAK RELWIRIRDA VKEVLDSTTL
EDLASYTDGE QEAYMFYI
