ID   SIGA_STRGR              Reviewed;         514 AA.
AC   P77951;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=RNA polymerase sigma factor SigA {ECO:0000255|HAMAP-Rule:MF_00963};
DE   AltName: Full=RNA polymerase principal sigma factor HrdB;
GN   Name=sigA {ECO:0000255|HAMAP-Rule:MF_00963}; Synonyms=hrdB;
OS   Streptomyces griseus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=2247;
RX   PubMed=8690707; DOI=10.1093/oxfordjournals.jbchem.a124935;
RA   Shinkawa H., Hatada Y., Okada M., Kinashi H., Nimi O.;
RT   "Nucleotide sequence of a principal sigma factor gene (hrdB) of
RT   Streptomyces griseus.";
RL   J. Biochem. 118:494-499(1995).
CC   -!- FUNCTION: Sigma factors are initiation factors that promote the
CC       attachment of RNA polymerase to specific initiation sites and are then
CC       released. This sigma factor is the primary sigma factor during
CC       exponential growth. {ECO:0000255|HAMAP-Rule:MF_00963}.
CC   -!- SUBUNIT: Interacts transiently with the RNA polymerase catalytic core.
CC       {ECO:0000255|HAMAP-Rule:MF_00963}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00963}.
CC   -!- SIMILARITY: Belongs to the sigma-70 factor family. RpoD/SigA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00963}.
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DR   EMBL; L08071; AAB16905.1; -; Genomic_DNA.
DR   RefSeq; WP_003965769.1; NZ_UAVD01000038.1.
DR   AlphaFoldDB; P77951; -.
DR   SMR; P77951; -.
DR   STRING; 1911.GCA_001715295_00082; -.
DR   PRIDE; P77951; -.
DR   GeneID; 6210716; -.
DR   OMA; QIPVTKW; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016987; F:sigma factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.10.10; -; 2.
DR   HAMAP; MF_00963; Sigma70_RpoD_SigA; 1.
DR   InterPro; IPR014284; RNA_pol_sigma-70_dom.
DR   InterPro; IPR000943; RNA_pol_sigma70.
DR   InterPro; IPR009042; RNA_pol_sigma70_r1_2.
DR   InterPro; IPR007627; RNA_pol_sigma70_r2.
DR   InterPro; IPR007624; RNA_pol_sigma70_r3.
DR   InterPro; IPR007630; RNA_pol_sigma70_r4.
DR   InterPro; IPR013325; RNA_pol_sigma_r2.
DR   InterPro; IPR013324; RNA_pol_sigma_r3/r4-like.
DR   InterPro; IPR012760; RNA_pol_sigma_RpoD_C.
DR   InterPro; IPR028630; Sigma70_RpoD.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   Pfam; PF00140; Sigma70_r1_2; 1.
DR   Pfam; PF04542; Sigma70_r2; 1.
DR   Pfam; PF04539; Sigma70_r3; 1.
DR   Pfam; PF04545; Sigma70_r4; 1.
DR   PRINTS; PR00046; SIGMA70FCT.
DR   SUPFAM; SSF88659; SSF88659; 2.
DR   SUPFAM; SSF88946; SSF88946; 1.
DR   TIGRFAMs; TIGR02393; RpoD_Cterm; 1.
DR   TIGRFAMs; TIGR02937; sigma70-ECF; 1.
DR   PROSITE; PS00715; SIGMA70_1; 1.
DR   PROSITE; PS00716; SIGMA70_2; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; DNA-binding; Sigma factor;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..514
FT                   /note="RNA polymerase sigma factor SigA"
FT                   /id="PRO_0000093992"
FT   DNA_BIND        475..494
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00963"
FT   REGION          135..205
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          281..351
FT                   /note="Sigma-70 factor domain-2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00963"
FT   REGION          360..436
FT                   /note="Sigma-70 factor domain-3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00963"
FT   REGION          449..502
FT                   /note="Sigma-70 factor domain-4"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00963"
FT   MOTIF           305..308
FT                   /note="Interaction with polymerase core subunit RpoC"
FT   COMPBIAS        136..155
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        156..193
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   514 AA;  56133 MW;  77873D66597C8A8D CRC64;
     MSASTSRTLP PEIAESESVM ALIERGKADG QIAGDDVRRA FEADQIPPTQ WKNVLRSLNQ
     ILEEEGVTLM VSAAESPKRA RKSVAAKSPV KRTATKTVAA KTTVTRTVAA TAAPAVESAD
     AADDAVAAAP AKKTAAKKAT AKKAAAKKTT AKKTAAKKSG KQDDEILDGD EAAEEVKAGK
     GEEEEGEGEN KGFVLSDDDE DDAPAQQVAV AGATADPVKD YLKQIGKVPL LNAEQEVELA
     KRIEAGLFAE DKLANADKLA PKLKRELEII AEDGRRAKNH LLEANLRLVV SLAKRYTGRG
     MLFLDLIQEG NLGLIRAVEK FDYTKGYKFS TYATWWIRQA ITRAMADQAR TIRIPVHMVE
     VINKLARVQR QMLQDLGREP TPEELAKELD MTPEKVIEVQ KYGREPISLH TPLGEDGDSE
     FGDLIEDSEA VVPADAVSFT LLQEQLHSVL DTLSEREAGV VSMRFGLTDG QPKTLDEIGK
     VYGVTRERIR QIESKTMSKL RHPSRSQVLR DYLD