RSGI_BACSU
ID RSGI_BACSU Reviewed; 381 AA.
AC O31655;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Anti-sigma-I factor RsgI {ECO:0000305};
DE AltName: Full=Regulation of sigma I protein {ECO:0000305};
GN Name=rsgI {ECO:0000303|PubMed:17185538}; Synonyms=ykrI;
GN OrderedLocusNames=BSU13460;
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 FUNCTION AS ANTI-FACTOR OF SIGI, INTERACTION WITH SIGI, AND INDUCTION.
RC STRAIN=168;
RX PubMed=17185538; DOI=10.1099/mic.0.29239-0;
RA Asai K., Ootsuji T., Obata K., Matsumoto T., Fujita Y., Sadaie Y.;
RT "Regulatory role of rsgI in sigI expression in Bacillus subtilis.";
RL Microbiology 153:92-101(2007).
RN [3]
RP DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=19114499; DOI=10.1128/jb.01497-08;
RA Schirner K., Errington J.;
RT "The cell wall regulator sigmaI specifically suppresses the lethal
RT phenotype of mbl mutants in Bacillus subtilis.";
RL J. Bacteriol. 191:1404-1413(2009).
RN [4]
RP INDUCTION.
RX PubMed=23199363; DOI=10.1111/mmi.12092;
RA Salzberg L.I., Powell L., Hokamp K., Botella E., Noone D., Devine K.M.;
RT "The WalRK (YycFG) and sigma(I) RsgI regulators cooperate to control CwlO
RT and LytE expression in exponentially growing and stressed Bacillus subtilis
RT cells.";
RL Mol. Microbiol. 87:180-195(2013).
RN [5]
RP INDUCTION.
RX PubMed=24125693; DOI=10.1016/j.resmic.2013.10.003;
RA Huang W.Z., Wang J.J., Chen H.J., Chen J.T., Shaw G.C.;
RT "The heat-inducible essential response regulator WalR positively regulates
RT transcription of sigI, mreBH and lytE in Bacillus subtilis under heat
RT stress.";
RL Res. Microbiol. 164:998-1008(2013).
CC -!- FUNCTION: Anti-sigma factor for SigI. Negatively regulates SigI
CC activity through direct interaction. {ECO:0000269|PubMed:17185538}.
CC -!- SUBUNIT: Interacts (via RsgI N-terminal anti-sigma domain) with SigI.
CC {ECO:0000255|PROSITE-ProRule:PRU01196, ECO:0000269|PubMed:17185538}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Part of the sigI-rsgI operon, which is transiently induced
CC by heat stress. Expression is positively regulated by SigI via the
CC sigma-I promoter (PubMed:17185538). In exponentially growing cells,
CC expression is regulated by the WalRK two-component system, which
CC represses the sigma-I promoter and activates the sigma-A promoter,
CC leading to the formation of a basal level of RsgI (PubMed:23199363).
CC WalRK can also positively and directly regulate transcription of the
CC operon under heat stress through a binding site located upstream of the
CC sigma-I promoter (PubMed:24125693). Repressed by glucose
CC (PubMed:17185538). {ECO:0000269|PubMed:17185538,
CC ECO:0000269|PubMed:23199363, ECO:0000269|PubMed:24125693}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene exhibit normal cell
CC morphology and growth rate at 37 degrees Celsius, however cell diameter
CC is slightly decreased. {ECO:0000269|PubMed:19114499}.
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DR EMBL; AL009126; CAB13219.1; -; Genomic_DNA.
DR PIR; E69862; E69862.
DR RefSeq; NP_389229.1; NC_000964.3.
DR RefSeq; WP_003244727.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; O31655; -.
DR SMR; O31655; -.
DR STRING; 224308.BSU13460; -.
DR PRIDE; O31655; -.
DR DNASU; 939360; -.
DR EnsemblBacteria; CAB13219; CAB13219; BSU_13460.
DR GeneID; 939360; -.
DR KEGG; bsu:BSU13460; -.
DR PATRIC; fig|224308.179.peg.1461; -.
DR eggNOG; ENOG5032YNU; Bacteria.
DR OMA; NQEGNNG; -.
DR BioCyc; BSUB:BSU13460-MON; -.
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; IPR024449; Anti-sigma_RsgI_N.
DR Pfam; PF12791; RsgI_N; 1.
DR PROSITE; PS51849; RSGI_N; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Reference proteome; Stress response;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..381
FT /note="Anti-sigma-I factor RsgI"
FT /id="PRO_0000379971"
FT TOPO_DOM 1..63
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 85..381
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT DOMAIN 2..50
FT /note="RsgI N-terminal anti-sigma"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01196"
FT REGION 198..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..357
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 381 AA; 43589 MW; E4BBC2674DAC99FE CRC64;
MRRGIIVEKN KKFVTLLTPD GQFLKAKNDR HSYEIGEEIM LPSETRMGRR ASFFDFFKLR
PFKMGIFTMT AIMLFIFIVL PVFSNNKAYA YMTIDINPSV EMALNSDYEV IELTPLNDEG
QKVVNDIDDW EKTDFKKVID DIITDCSEHG YVKKSKEILI STVYENTEDN TYKKAVKKQL
NDVTEKYKTT YRMESLESDM QTREKAKKEG VSTGSYIKSN EKNDNKDIKD DSSKPSGEED
QKSDENEDEN TDQTDTQDSK QGDNEQLNDA DSGDQKEEKA DDQIDDSDKD KKIKESDENT
NTEKDGDHEQ TPIQDPQDKG NENNGADKGQ SQYHRDWNNG EQGKNRSSSR RDNASDRRNP
NGYSSDNHSA KNEDSPSAPG E
