ID   SIGX_BACSU              Reviewed;         194 AA.
AC   P35165;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 2.
DT   03-AUG-2022, entry version 148.
DE   RecName: Full=ECF RNA polymerase sigma factor SigX;
DE            Short=ECF sigma factor SigX;
GN   Name=sigX; Synonyms=ypuM; OrderedLocusNames=BSU23100;
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 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC   3610 / NRRL NRS-744 / VKM B-501;
RX   PubMed=7934829; DOI=10.1111/j.1365-2958.1993.tb02670.x;
RA   Sorokin A.V., Zumstein E., Azevedo V., Ehrlich S.D., Serror P.;
RT   "The organization of the Bacillus subtilis 168 chromosome region between
RT   the spoVA and serA genetic loci, based on sequence data.";
RL   Mol. Microbiol. 10:385-395(1993).
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 112-113.
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   POSSIBLE FUNCTION.
RX   PubMed=8052622; DOI=10.1073/pnas.91.16.7573;
RA   Lonetto M.A., Brown K.L., Rudd K.E., Buttner M.J.;
RT   "Analysis of the Streptomyces coelicolor sigE gene reveals the existence of
RT   a subfamily of eubacterial RNA polymerase sigma factors involved in the
RT   regulation of extracytoplasmic functions.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:7573-7577(1994).
RN   [5]
RP   CHARACTERIZATION.
RX   PubMed=9393439; DOI=10.1007/s004380050585;
RA   Brutsche S., Braun V.;
RT   "SigX of Bacillus subtilis replaces the ECF sigma factor fecI of
RT   Escherichia coli and is inhibited by RsiX.";
RL   Mol. Gen. Genet. 256:416-425(1997).
RN   [6]
RP   FUNCTION, SUBUNIT, AND INDUCTION.
RC   STRAIN=168;
RX   PubMed=21710567; DOI=10.1002/pmic.201000790;
RA   Delumeau O., Lecointe F., Muntel J., Guillot A., Guedon E., Monnet V.,
RA   Hecker M., Becher D., Polard P., Noirot P.;
RT   "The dynamic protein partnership of RNA polymerase in Bacillus subtilis.";
RL   Proteomics 11:2992-3001(2011).
RN   [7]
RP   INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=168;
RX   PubMed=22211522; DOI=10.1111/j.1365-2958.2011.07953.x;
RA   Luo Y., Helmann J.D.;
RT   "Analysis of the role of Bacillus subtilis sigma(M) in beta-lactam
RT   resistance reveals an essential role for c-di-AMP in peptidoglycan
RT   homeostasis.";
RL   Mol. Microbiol. 83:623-639(2012).
CC   -!- FUNCTION: Sigma factors are initiation factors that promote the
CC       attachment of RNA polymerase (RNAP) to specific initiation sites and
CC       are then released. May be involved in the regulation of iron
CC       metabolism. Associates with RNAP core during early growth phases,
CC       association decreases as cells age (PubMed:21710567).
CC       {ECO:0000269|PubMed:21710567}.
CC   -!- SUBUNIT: Interacts transiently with the RNAP core.
CC       {ECO:0000305|PubMed:21710567}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC   -!- INDUCTION: Induced 3-fold by the beta-lactam antibiotic cefuroxime.
CC       {ECO:0000269|PubMed:22211522}.
CC   -!- DISRUPTION PHENOTYPE: No effect on antibiotic resistance; double sigM-
CC       sigX mutants have 130-fold increases sensitivity to the beta-lactam
CC       antibiotic cefuroxime (PubMed:22211522). Association with RNAP core
CC       increases during many stresses (at protein level) (PubMed:21710567).
CC       {ECO:0000269|PubMed:21710567, ECO:0000269|PubMed:22211522}.
CC   -!- SIMILARITY: Belongs to the sigma-70 factor family. ECF subfamily.
CC       {ECO:0000305}.
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DR   EMBL; L09228; AAA67499.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14242.2; -; Genomic_DNA.
DR   PIR; S45561; S45561.
DR   RefSeq; NP_390191.2; NC_000964.3.
DR   RefSeq; WP_003230521.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; P35165; -.
DR   SMR; P35165; -.
DR   IntAct; P35165; 1.
DR   STRING; 224308.BSU23100; -.
DR   PaxDb; P35165; -.
DR   PRIDE; P35165; -.
DR   EnsemblBacteria; CAB14242; CAB14242; BSU_23100.
DR   GeneID; 938966; -.
DR   KEGG; bsu:BSU23100; -.
DR   eggNOG; COG1595; Bacteria.
DR   InParanoid; P35165; -.
DR   OMA; SNQRRWW; -.
DR   PhylomeDB; P35165; -.
DR   BioCyc; BSUB:BSU23100-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0016987; F:sigma factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro.
DR   GO; GO:0006950; P:response to stress; IEA:UniProt.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR039425; RNA_pol_sigma-70-like.
DR   InterPro; IPR014284; RNA_pol_sigma-70_dom.
DR   InterPro; IPR000838; RNA_pol_sigma70_ECF_CS.
DR   InterPro; IPR007627; RNA_pol_sigma70_r2.
DR   InterPro; IPR013249; RNA_pol_sigma70_r4_t2.
DR   InterPro; IPR013325; RNA_pol_sigma_r2.
DR   InterPro; IPR013324; RNA_pol_sigma_r3/r4-like.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR43133; PTHR43133; 1.
DR   Pfam; PF04542; Sigma70_r2; 1.
DR   Pfam; PF08281; Sigma70_r4_2; 1.
DR   SUPFAM; SSF88659; SSF88659; 1.
DR   SUPFAM; SSF88946; SSF88946; 1.
DR   TIGRFAMs; TIGR02937; sigma70-ECF; 1.
DR   PROSITE; PS01063; SIGMA70_ECF; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; DNA-binding; Membrane; Reference proteome; Sigma factor;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..194
FT                   /note="ECF RNA polymerase sigma factor SigX"
FT                   /id="PRO_0000094017"
FT   DNA_BIND        136..155
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000250"
FT   MOTIF           32..45
FT                   /note="Polymerase core binding"
FT   CONFLICT        112..113
FT                   /note="YA -> SC (in Ref. 1; AAA67499)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   194 AA;  23223 MW;  AB95D111573676BC CRC64;
     MEETFQLLYD TYHQDLYQFL FYMVKDKNQT EDLLQEVYIR VLNSYHTFEG RSSEKTWLLS
     IARHVAIDWF RKQQTIRQRI LGTFDWDTQD VRDQQLLPDE LAVQHENVRE IYAALDQCTI
     DQRAVIILRF IQGYSIQETA KALRFSESKV KTTQHRGLKV LRKHMELLRE ELMDDEVRME
     RRTDKGVVKS TSGS