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Database: UniProt
Entry: A0A5C5ULF5_9BACL
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ID   A0A5C5ULF5_9BACL        Unreviewed;       384 AA.
AC   A0A5C5ULF5;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2019, sequence version 1.
DT   18-JUN-2025, entry version 19.
DE   RecName: Full=RNA polymerase sigma factor SigA {ECO:0000256|HAMAP-Rule:MF_00963};
GN   Name=rpoD {ECO:0000313|EMBL:TWT26175.1};
GN   Synonyms=sigA {ECO:0000256|HAMAP-Rule:MF_00963};
GN   ORFNames=FQV30_10345 {ECO:0000313|EMBL:TWT26175.1};
OS   Planomicrobium sp. CPCC 101110.
OC   Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Caryophanaceae;
OC   Planomicrobium.
OX   NCBI_TaxID=2599619 {ECO:0000313|EMBL:TWT26175.1, ECO:0000313|Proteomes:UP000316502};
RN   [1] {ECO:0000313|EMBL:TWT26175.1, ECO:0000313|Proteomes:UP000316502}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CPCC 101110 {ECO:0000313|EMBL:TWT26175.1,
RC   ECO:0000313|Proteomes:UP000316502};
RA   Zhang Y., Shi Y.;
RT   "Whole genome sequence of Planomicrobium sp. CPCC 101110T.";
RL   Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_00963}.
CC   -!- SUBUNIT: Interacts transiently with the RNA polymerase catalytic core.
CC       {ECO:0000256|HAMAP-Rule:MF_00963}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00963}.
CC   -!- SIMILARITY: Belongs to the sigma-70 factor family. RpoD/SigA subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00963}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:TWT26175.1}.
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DR   EMBL; VOHD01000006; TWT26175.1; -; Genomic_DNA.
DR   RefSeq; WP_146500089.1; NZ_VOHD01000006.1.
DR   AlphaFoldDB; A0A5C5ULF5; -.
DR   OrthoDB; 9809557at2; -.
DR   Proteomes; UP000316502; Unassembled WGS sequence.
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   CDD; cd06171; Sigma70_r4; 1.
DR   FunFam; 1.10.10.10:FF:000002; RNA polymerase sigma factor SigA; 1.
DR   FunFam; 1.10.10.10:FF:000004; RNA polymerase sigma factor SigA; 1.
DR   FunFam; 1.10.601.10:FF:000001; RNA polymerase sigma factor SigA; 1.
DR   Gene3D; 1.10.601.10; RNA Polymerase Primary Sigma Factor; 2.
DR   Gene3D; 1.10.220.120; Sigma-70 factor, region 1.1; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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; IPR007127; RNA_pol_sigma_70_r1_1.
DR   InterPro; IPR042189; RNA_pol_sigma_70_r1_1_sf.
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; IPR050239; Sigma-70_RNA_pol_init_factors.
DR   InterPro; IPR028630; Sigma70_RpoD.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   NCBIfam; NF006666; PRK09210.1; 1.
DR   NCBIfam; TIGR02393; RpoD_Cterm; 1.
DR   NCBIfam; TIGR02937; sigma70-ECF; 1.
DR   PANTHER; PTHR30603; RNA POLYMERASE SIGMA FACTOR RPO; 1.
DR   PANTHER; PTHR30603:SF60; RNA POLYMERASE SIGMA FACTOR RPOD; 1.
DR   Pfam; PF03979; Sigma70_r1_1; 1.
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; SSF88946; Sigma2 domain of RNA polymerase sigma factors; 1.
DR   SUPFAM; SSF88659; Sigma3 and sigma4 domains of RNA polymerase sigma factors; 2.
DR   PROSITE; PS00715; SIGMA70_1; 1.
DR   PROSITE; PS00716; SIGMA70_2; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00963};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00963}; Reference proteome {ECO:0000313|Proteomes:UP000316502};
KW   Sigma factor {ECO:0000256|ARBA:ARBA00023082, ECO:0000256|HAMAP-
KW   Rule:MF_00963};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW   Rule:MF_00963};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015, ECO:0000256|HAMAP-
KW   Rule:MF_00963}.
FT   DOMAIN          175..188
FT                   /note="RNA polymerase sigma-70"
FT                   /evidence="ECO:0000259|PROSITE:PS00715"
FT   DOMAIN          344..370
FT                   /note="RNA polymerase sigma-70"
FT                   /evidence="ECO:0000259|PROSITE:PS00716"
FT   DNA_BIND        345..364
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          151..221
FT                   /note="Sigma-70 factor domain-2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   REGION          230..306
FT                   /note="Sigma-70 factor domain-3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   REGION          319..372
FT                   /note="Sigma-70 factor domain-4"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   COILED          306..333
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOTIF           175..178
FT                   /note="Interaction with polymerase core subunit RpoC"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   COMPBIAS        1..10
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   384 AA;  44121 MW;  62420BAAB70CD688 CRC64;
     MAEKSERPNE VETSNAPLTI EGPEAGIEEA KRQLIEIGKK TGELNYEQIA DKLAVFEMES
     DQVEEFIDQL EGHGIELERK TDDEEHLDRL MKPTEEKFDL NDLSVPPGVK INDPVRMYLK
     EIGRVDLLKA EEEVRLAKLI EQGDEEAKKR LAEANLRLVV SIAKRYVGRG MLFLDLIQEG
     NMGLIKAVEK FDYSKGFKFS TYATWWIRQA ITRAIADQAR TIRIPVHMVE TINKLIRVQR
     QLLQDLGREP SPEEIGEEMD LLPEKVREIL KIAQEPVSLE TPIGEEDDSH LGDFIEDSDA
     QSPSDHAAYE LLKEQLEDVL DTLTDREENV LRLRFGLDDG RTRTLEEVGK VFGVTRERIR
     QIEAKALRKL RHPSRSKRLK DFLE
//
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