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SIGG_MYCTO
ID   SIGG_MYCTO              Reviewed;         370 AA.
AC   P9WGG4; L7N5U5;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=ECF RNA polymerase sigma factor SigG;
DE            Short=ECF sigma factor SigG;
DE   AltName: Full=Alternative RNA polymerase sigma factor SigG;
DE   AltName: Full=RNA polymerase sigma-G factor;
DE            Short=Sigma-g factor;
GN   Name=sigG; OrderedLocusNames=MT0191;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
RN   [2]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND REGULON.
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=18039768; DOI=10.1128/jb.00511-07;
RA   Lee J.H., Geiman D.E., Bishai W.R.;
RT   "Role of stress response sigma factor SigG in Mycobacterium tuberculosis.";
RL   J. Bacteriol. 190:1128-1133(2008).
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 a cognate anti-sigma factor until released, although
CC       no anti-sigma factor is known for this protein. May be involved in host
CC       intracellular survival after infection (strains H37Rv and CDC 1551). A
CC       role in the SOS response is controversial; it has been seen in strain
CC       CDC 1551 (PubMed:18039768) but not in H37Rv (PubMed:21169493).
CC       {ECO:0000269|PubMed:18039768}.
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. {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 (By similarity). {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Not essential. Slight repression of sigH, sigF,
CC       and lexA, slight induction of sigD. Increased resistance to mitomycin
CC       C, reduced survival in mouse-derived J774A.1 macrophages after 6 days
CC       growth (PubMed:18039768). {ECO:0000269|PubMed:18039768}.
CC   -!- SIMILARITY: Belongs to the sigma-70 factor family. ECF subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE000516; AAK44411.1; -; Genomic_DNA.
DR   PIR; A70906; A70906.
DR   RefSeq; WP_003401110.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WGG4; -.
DR   SMR; P9WGG4; -.
DR   EnsemblBacteria; AAK44411; AAK44411; MT0191.
DR   KEGG; mtc:MT0191; -.
DR   PATRIC; fig|83331.31.peg.208; -.
DR   HOGENOM; CLU_043648_0_0_11; -.
DR   Proteomes; UP000001020; 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   GO; GO:0006950; P:response to stress; IEA:UniProt.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR032710; NTF2-like_dom_sf.
DR   InterPro; IPR039425; RNA_pol_sigma-70-like.
DR   InterPro; IPR014284; RNA_pol_sigma-70_dom.
DR   InterPro; IPR014305; RNA_pol_sigma-G_actinobac.
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; IPR037401; SnoaL-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   Pfam; PF12680; SnoaL_2; 1.
DR   SUPFAM; SSF54427; SSF54427; 1.
DR   SUPFAM; SSF88659; SSF88659; 1.
DR   SUPFAM; SSF88946; SSF88946; 1.
DR   TIGRFAMs; TIGR02937; sigma70-ECF; 1.
DR   TIGRFAMs; TIGR02960; SigX5; 1.
DR   PROSITE; PS01063; SIGMA70_ECF; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Sigma factor; Transcription; Transcription regulation.
FT   CHAIN           1..370
FT                   /note="ECF RNA polymerase sigma factor SigG"
FT                   /id="PRO_0000428366"
FT   DNA_BIND        207..226
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000250"
FT   REGION          63..129
FT                   /note="Sigma-70 factor domain-2"
FT   REGION          180..232
FT                   /note="Sigma-70 factor domain-4"
FT   MOTIF           85..88
FT                   /note="Polymerase core binding"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   370 AA;  40983 MW;  DF6CA9852FF3A793 CRC64;
     MRTSPMPAKF RSVRVVVITG SVTAAPVRVS ETLRRLIDVS VLAENSGREP ADERRGDFSA
     HTEPYRRELL AHCYRMTGSL HDAEDLVQET LLRAWKAYEG FAGKSSLRTW LHRIATNTCL
     TALEGRRRRP LPTGLGRPSA DPSGELVERR EVSWLEPLPD VTDDPADPST IVGNRESVRL
     AFVAALQHLS PRQRAVLLLR DVLQWKSAEV ADAIGTSTVA VNSLLQRARS QLQTVRPSAA
     DRLSAPDSPE AQDLLARYIA AFEAYDIDRL VELFTAEAIW EMPPYTGWYQ GAQAIVTLIH
     QQCPAYSPGD MRLISLIANG QPAAAMYMRA GDVHLPFQLH VLDMAADRVS HVVAFLDTTL
     FPKFGLPDSL
 
 
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