MGSR_BACSU
ID MGSR_BACSU Reviewed; 126 AA.
AC P54503;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Regulatory protein MgsR {ECO:0000305};
DE AltName: Full=Modulator of the general stress response {ECO:0000303|PubMed:18643936};
GN Name=mgsR {ECO:0000303|PubMed:18643936}; Synonyms=yqgZ;
GN OrderedLocusNames=BSU24770;
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 / JH642;
RX PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA Kobayashi Y.;
RT "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT Bacillus subtilis genome containing the skin element and many sporulation
RT genes.";
RL Microbiology 142:3103-3111(1996).
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 SEQUENCE REVISION TO 77.
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 [4]
RP INDUCTION.
RX PubMed=11544224; DOI=10.1128/jb.183.19.5617-5631.2001;
RA Petersohn A., Brigulla M., Haas S., Hoheisel J.D., Voelker U., Hecker M.;
RT "Global analysis of the general stress response of Bacillus subtilis.";
RL J. Bacteriol. 183:5617-5631(2001).
RN [5]
RP FUNCTION, INDUCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF CYS-13 AND
RP GLY-55, AND GENE NAME.
RX PubMed=18643936; DOI=10.1111/j.1365-2958.2008.06332.x;
RA Reder A., Hoper D., Weinberg C., Gerth U., Fraunholz M., Hecker M.;
RT "The Spx paralogue MgsR (YqgZ) controls a subregulon within the general
RT stress response of Bacillus subtilis.";
RL Mol. Microbiol. 69:1104-1120(2008).
RN [6]
RP ACTIVITY REGULATION, INDUCTION, DISULFIDE BOND, AND MUTAGENESIS OF CYS-13
RP AND GLY-55.
RX PubMed=22812682; DOI=10.1111/j.1462-2920.2012.02829.x;
RA Reder A., Poether D.C., Gerth U., Hecker M.;
RT "The modulator of the general stress response, MgsR, of Bacillus subtilis
RT is subject to multiple and complex control mechanisms.";
RL Environ. Microbiol. 14:2838-2850(2012).
RN [7]
RP ACTIVITY REGULATION, AND MUTAGENESIS OF ARG-17; ARG-33; ARG-37; ARG-42;
RP ARG-63 AND 94-ARG-ARG-95.
RX PubMed=32477307; DOI=10.3389/fmicb.2020.00900;
RA Lilge L., Reder A., Tippmann F., Morgenroth F., Grohmann J., Becher D.,
RA Riedel K., Voelker U., Hecker M., Gerth U.;
RT "The involvement of the McsB arginine kinase in Clp-dependent degradation
RT of the MgsR regulator in Bacillus subtilis.";
RL Front. Microbiol. 11:900-900(2020).
CC -!- FUNCTION: Regulates transcription of a subregulon within the general
CC stress response (PubMed:18643936). Exerts positive and negative effects
CC in response to ethanol stress (PubMed:18643936).
CC {ECO:0000269|PubMed:18643936}.
CC -!- ACTIVITY REGULATION: Activity is controlled at multiple levels
CC (PubMed:22812682). Regulation includes a positive autoregulatory loop
CC on mgsR transcription and a post-translational redox-sensitive
CC activation step by an intramolecular disulfide bond formation in
CC response to ethanol stress (PubMed:22812682). In addition, protein
CC stability is strictly controlled by rapid proteolytic degradation by
CC the ClpXP and ClpCP proteases (PubMed:22812682, PubMed:32477307). The
CC McsB protein-arginine kinase might serve as a proteolytic adapter for
CC the ClpX ATPase in the degradation mechanism of MgsR (PubMed:32477307).
CC {ECO:0000269|PubMed:22812682, ECO:0000269|PubMed:32477307}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Expression is sigma B-dependent (PubMed:11544224,
CC PubMed:18643936). Induced by ethanol, heat and salt stress
CC (PubMed:11544224, PubMed:18643936). Positively autoregulated
CC (PubMed:22812682). {ECO:0000269|PubMed:11544224,
CC ECO:0000269|PubMed:18643936, ECO:0000269|PubMed:22812682}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene results in differential
CC expression of approximately 70 genes in response to ethanol stress
CC compared with the wild-type strain. {ECO:0000269|PubMed:18643936}.
CC -!- SIMILARITY: Belongs to the ArsC family. {ECO:0000305}.
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DR EMBL; D84432; BAA12529.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14408.2; -; Genomic_DNA.
DR PIR; C69958; C69958.
DR RefSeq; NP_390357.2; NC_000964.3.
DR RefSeq; WP_003230147.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P54503; -.
DR SMR; P54503; -.
DR STRING; 224308.BSU24770; -.
DR PaxDb; P54503; -.
DR PRIDE; P54503; -.
DR EnsemblBacteria; CAB14408; CAB14408; BSU_24770.
DR GeneID; 938484; -.
DR KEGG; bsu:BSU24770; -.
DR PATRIC; fig|224308.179.peg.2696; -.
DR eggNOG; COG1393; Bacteria.
DR InParanoid; P54503; -.
DR OMA; RMFIPRE; -.
DR PhylomeDB; P54503; -.
DR BioCyc; BSUB:BSU24770-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR InterPro; IPR006660; Arsenate_reductase-like.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR006504; Tscrpt_reg_Spx/MgsR.
DR PANTHER; PTHR30041; PTHR30041; 1.
DR Pfam; PF03960; ArsC; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR01617; arsC_related; 1.
DR PROSITE; PS51353; ARSC; 1.
PE 1: Evidence at protein level;
KW Activator; Cytoplasm; Disulfide bond; Redox-active center;
KW Reference proteome; Repressor; Stress response; Transcription;
KW Transcription regulation.
FT CHAIN 1..126
FT /note="Regulatory protein MgsR"
FT /id="PRO_0000162583"
FT DISULFID 13..16
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01282,
FT ECO:0000269|PubMed:22812682"
FT MUTAGEN 13
FT /note="C->S: Loss of activity. Strongly diminishes
FT expression of mgsR and of the MgsR regulon."
FT /evidence="ECO:0000269|PubMed:18643936,
FT ECO:0000269|PubMed:22812682"
FT MUTAGEN 17
FT /note="R->E: Destabilizes MgsR approximately by half.
FT Almost loss of activity."
FT /evidence="ECO:0000269|PubMed:32477307"
FT MUTAGEN 33
FT /note="R->E: Strong decrease in MgsR stability. Strong
FT decrease in activity."
FT /evidence="ECO:0000269|PubMed:32477307"
FT MUTAGEN 37
FT /note="R->E: Destabilizes MgsR approximately by half.
FT Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:32477307"
FT MUTAGEN 42
FT /note="R->E: Destabilizes MgsR approximately by half. No
FT change in activity."
FT /evidence="ECO:0000269|PubMed:32477307"
FT MUTAGEN 55
FT /note="G->R: Loss of activity. Strongly diminishes
FT expression of mgsR and of the MgsR regulon."
FT /evidence="ECO:0000269|PubMed:18643936,
FT ECO:0000269|PubMed:22812682"
FT MUTAGEN 63
FT /note="R->E: Slight increase in MgsR stability. Strong
FT decrease in activity."
FT /evidence="ECO:0000269|PubMed:32477307"
FT MUTAGEN 94..95
FT /note="RR->EE: Strong decrease in MgsR stability. Almost
FT loss of activity."
FT /evidence="ECO:0000269|PubMed:32477307"
FT CONFLICT 77
FT /note="M -> I (in Ref. 1; BAA12529)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 126 AA; 14842 MW; AD1556A2B10DE10E CRC64;
MEQQLTFYSY PSCTSCRKTK HWLKAHQIEF NERHLFRETP TREELKYILS LTTEGIDEIL
ATRSQTFKNL NLNIEEMTVN EVLELLIEKP KLLRRPILVD NKKLVIGYNP GELLKLSKKK
TVHQSA
