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SIGM_MYCTE
ID   SIGM_MYCTE              Reviewed;         196 AA.
AC   H8F2P4;
DT   26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2012, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=ECF RNA polymerase sigma factor SigM;
DE            Short=ECF sigma factor SigM;
DE   AltName: Full=Alternative RNA polymerase sigma factor SigM;
DE   AltName: Full=RNA polymerase sigma-M factor;
DE            Short=Sigma-M factor;
GN   Name=sigM; OrderedLocusNames=ERDMAN_4291;
OS   Mycobacterium tuberculosis (strain ATCC 35801 / TMC 107 / Erdman).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=652616;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX   PubMed=22535945; DOI=10.1128/jb.00353-12;
RA   Miyoshi-Akiyama T., Matsumura K., Iwai H., Funatogawa K., Kirikae T.;
RT   "Complete annotated genome sequence of Mycobacterium tuberculosis Erdman.";
RL   J. Bacteriol. 194:2770-2770(2012).
RN   [2]
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX   PubMed=20545848; DOI=10.1111/j.1365-2958.2010.07232.x;
RA   Sklar J.G., Makinoshima H., Schneider J.S., Glickman M.S.;
RT   "M. tuberculosis intramembrane protease Rip1 controls transcription through
RT   three anti-sigma factor substrates.";
RL   Mol. Microbiol. 77:605-617(2010).
CC   -!- FUNCTION: Sigma factors are initiation factors that promote the
CC       attachment of RNA polymerase to specific initiation sites and are then
CC       released. Extracytoplasmic function (ECF) sigma factors are held in an
CC       inactive form by an anti-sigma factor until released by regulated
CC       intramembrane proteolysis (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts transiently with the RNA polymerase catalytic core
CC       formed by RpoA, RpoB, RpoC and RpoZ (2 alpha, 1 beta, 1 beta' and 1
CC       omega subunit) to form the RNA polymerase holoenzyme that can initiate
CC       transcription. Interacts (via sigma-70 factor domain 4) with anti-
CC       sigma-M factor RsmA (By similarity). {ECO:0000250}.
CC   -!- DOMAIN: The sigma-70 factor domain-2 mediates sequence-specific
CC       interaction with the -10 element in promoter DNA, and plays an
CC       important role in melting the double-stranded DNA and the formation of
CC       the transcription bubble. The sigma-70 factor domain-2 mediates
CC       interaction with the RNA polymerase subunits RpoB and RpoC (By
CC       similarity). {ECO:0000250}.
CC   -!- DOMAIN: The sigma-70 factor domain-4 contains a helix-turn-helix (H-T-
CC       H) motif that mediates interaction with the -35 element in promoter
CC       DNA. The domain also mediates interaction with the RNA polymerase
CC       subunit RpoA. Interactions between sigma-70 factor domain-4 and anti-
CC       sigma factors prevents interaction of sigma factors with the RNA
CC       polymerase catalytic core (By similarity). {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: No effect on phenanthroline induction of katG.
CC       {ECO:0000269|PubMed:20545848}.
CC   -!- MISCELLANEOUS: Extracytoplasmic function (ECF) sigma factors are held
CC       in an inactive form by an anti-sigma factor until released by regulated
CC       intramembrane proteolysis (RIP). RIP occurs when an extracytoplasmic
CC       signal triggers a concerted proteolytic cascade to transmit information
CC       and elicit cellular responses. The membrane-spanning anti-sigma factor
CC       is first cut extracytoplasmically (site-1 protease, S1P), then within
CC       the membrane itself (site-2 protease, S2P, Rip1), while cytoplasmic
CC       proteases finish degrading the regulatory protein, liberating SigM
CC       (Probable). {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the sigma-70 factor family. ECF subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AP012340; BAL68055.1; -; Genomic_DNA.
DR   RefSeq; WP_003899761.1; NZ_KK339488.1.
DR   AlphaFoldDB; H8F2P4; -.
DR   SMR; H8F2P4; -.
DR   EnsemblBacteria; BAL68055; BAL68055; ERDMAN_4291.
DR   KEGG; mtn:ERDMAN_4291; -.
DR   PATRIC; fig|652616.3.peg.4373; -.
DR   HOGENOM; CLU_047691_3_0_11; -.
DR   Proteomes; UP000007568; Chromosome.
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:0009628; P:response to abiotic stimulus; 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; 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.
PE   3: Inferred from homology;
KW   DNA-binding; Sigma factor; Transcription; Transcription regulation.
FT   CHAIN           1..196
FT                   /note="ECF RNA polymerase sigma factor SigM"
FT                   /id="PRO_0000422694"
FT   DNA_BIND        156..175
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255"
FT   REGION          39..105
FT                   /note="Sigma-70 factor domain-2"
FT   REGION          130..181
FT                   /note="Sigma-70 factor domain-4"
FT   MOTIF           63..66
FT                   /note="Interaction with polymerase core subunit RpoC"
SQ   SEQUENCE   196 AA;  21648 MW;  677B7FEFEBC619F0 CRC64;
     MPPPIGYCPA VGFGGRHERS NAELLAAHVA GDRYAFDQLF RRHHRQLHRL ARLTSRTSED
     ADDALQDAML SAHRGAGSFR YDAAVSSWLH RIVVNACLDR LRRAKAHPTA PLEDVYPVAD
     RTAQVETAIA VQRALMRLPV EQRAAVVAVD MQGYSIADTA RMLGVAEGTV KSRCARARAR
     LARLLGYLNT GVNIRR
 
 
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