ID   SIGE_MYCTE              Reviewed;         257 AA.
AC   H8F0N6;
DT   24-JUL-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 SigE;
DE            Short=ECF sigma factor SigE;
DE   AltName: Full=Alternative RNA polymerase sigma factor SigE;
DE   AltName: Full=RNA polymerase sigma-E factor;
DE            Short=Sigma-E factor;
GN   Name=sigE; OrderedLocusNames=ERDMAN_1366;
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   INDUCTION.
RC   STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX   PubMed=11373121; DOI=10.1006/mpat.2001.0431;
RA   Jensen-Cain D.M., Quinn F.D.;
RT   "Differential expression of sigE by Mycobacterium tuberculosis during
RT   intracellular growth.";
RL   Microb. Pathog. 30:271-278(2001).
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. Responds to
CC       surface stress (H(2)O(2)) (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 cognate
CC       anti-sigma-E factor RseA under reducing conditions, which stops the
CC       sigma factor from functioning (By similarity). {ECO:0000250}.
CC   -!- INDUCTION: Not expressed in liquid culture (in vitro), induced by
CC       H(2)O(2) (at protein level). Expressed 6 hours after infection of human
CC       macrophages, expression continues for at least 5 days.
CC       {ECO:0000269|PubMed:11373121}.
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   -!- SIMILARITY: Belongs to the sigma-70 factor family. ECF subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AP012340; BAL65169.1; -; Genomic_DNA.
DR   RefSeq; WP_003406257.1; NZ_KK339487.1.
DR   AlphaFoldDB; H8F0N6; -.
DR   SMR; H8F0N6; -.
DR   PRIDE; H8F0N6; -.
DR   EnsemblBacteria; BAL65169; BAL65169; ERDMAN_1366.
DR   GeneID; 45425191; -.
DR   KEGG; mtn:ERDMAN_1366; -.
DR   PATRIC; fig|652616.3.peg.1387; -.
DR   HOGENOM; CLU_047691_1_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   1: Evidence at protein level;
KW   DNA-binding; Sigma factor; Transcription; Transcription regulation.
FT   CHAIN           1..257
FT                   /note="ECF RNA polymerase sigma factor SigE"
FT                   /id="PRO_0000422947"
FT   DNA_BIND        211..230
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000250"
FT   REGION          87..153
FT                   /note="Sigma-70 factor domain-2"
FT   REGION          186..236
FT                   /note="Sigma-70 factor domain-4"
FT   MOTIF           111..114
FT                   /note="Polymerase core binding"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   257 AA;  28877 MW;  E7AB77CAECBF6CE7 CRC64;
     MELLGGPRVG NTESQLCVAD GDDLPTYCSA NSEDLNITTI TTLSPTSMSH PQQVRDDQWV
     EPSDQLQGTA VFDATGDKAT MPSWDELVRQ HADRVYRLAY RLSGNQHDAE DLTQETFIRV
     FRSVQNYQPG TFEGWLHRIT TNLFLDMVRR RARIRMEALP EDYDRVPADE PNPEQIYHDA
     RLGPDLQAAL ASLPPEFRAA VVLCDIEGLS YEEIGATLGV KLGTVRSRIH RGRQALRDYL
     AAHPEHGECA VHVNPVR