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Database: UniProt
Entry: A0A5K8A4L0_9BACT
LinkDB: A0A5K8A4L0_9BACT
Original site: A0A5K8A4L0_9BACT 
ID   A0A5K8A4L0_9BACT        Unreviewed;       620 AA.
AC   A0A5K8A4L0;
DT   26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2020, sequence version 1.
DT   18-JUN-2025, entry version 21.
DE   RecName: Full=RNA polymerase sigma factor SigA {ECO:0000256|HAMAP-Rule:MF_00963};
GN   Name=rpoD {ECO:0000313|EMBL:BBO87449.1};
GN   Synonyms=sigA {ECO:0000256|HAMAP-Rule:MF_00963};
GN   ORFNames=DSCOOX_06290 {ECO:0000313|EMBL:BBO87449.1};
OS   Desulfosarcina ovata subsp. ovata.
OC   Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
OC   Desulfobacterales; Desulfosarcinaceae; Desulfosarcina.
OX   NCBI_TaxID=2752305 {ECO:0000313|EMBL:BBO87449.1, ECO:0000313|Proteomes:UP000422108};
RN   [1] {ECO:0000313|EMBL:BBO87449.1, ECO:0000313|Proteomes:UP000422108}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=oXyS1 {ECO:0000313|Proteomes:UP000422108};
RA   Watanabe M., Kojima H., Fukui M.;
RT   "Comparative genomics of hydrocarbon-degrading Desulfosarcina strains.";
RL   Submitted (NOV-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}.
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DR   EMBL; AP021879; BBO87449.1; -; Genomic_DNA.
DR   RefSeq; WP_155308903.1; NZ_AP021879.1.
DR   AlphaFoldDB; A0A5K8A4L0; -.
DR   Proteomes; UP000422108; Chromosome.
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; 1.
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; NF004208; PRK05658.1; 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   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:UP000422108};
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          410..423
FT                   /note="RNA polymerase sigma-70"
FT                   /evidence="ECO:0000259|PROSITE:PS00715"
FT   DOMAIN          579..605
FT                   /note="RNA polymerase sigma-70"
FT                   /evidence="ECO:0000259|PROSITE:PS00716"
FT   DNA_BIND        580..599
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          386..456
FT                   /note="Sigma-70 factor domain-2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   REGION          465..541
FT                   /note="Sigma-70 factor domain-3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   REGION          554..607
FT                   /note="Sigma-70 factor domain-4"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   MOTIF           410..413
FT                   /note="Interaction with polymerase core subunit RpoC"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   COMPBIAS        1..20
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   620 AA;  71366 MW;  18C010E60B8D4659 CRC64;
     MTKQSDDKRK AASSREEKKT AQKPVEAAGD AAVQDVKSEK SKPLSKKSNQ KALKALIEKG
     KEQGSLTYDE INEALPNEMM SSEMIDDTLM MFDDMDIEII ENEDGIPGKD STPEKKEALN
     KAVSVSDFGS VTDPVKMYLR EMGMVTLLSR EGEVEIAKKI EEGEQDVLKA LLETSLGVKY
     ILEFGDLIEK GALRPKHVLR DVDEGDAYVD EMVQIDNFLN TITEIRKVDE ENQQYRERMF
     TEQLDPDEAR RVRRCIMRRN NKIFDLLKGW RLEGGVIDRI EVHIRRLIDW FDAQNRLVAT
     TAEAMGTTIR ELRENIEEKS GFLAWARVKS SLDDTALGRI YDHLRSVSDL LVEKENDFKA
     NNRNLKRVMA SVDEGRLRAK FAKSELIRAN LRLVVSIAKK YTNRGLQFLD LIQEGNIGLM
     KAVDKFEYRR GYKFSTYATW WIRQAITRAI ADQARTIRIP VHMIETINKL IRTSRYLVQE
     FGREPRPEEI AEKMEIPIDK VRKVLKIARE PISLETPIGE EEDSHLGDFI EDKKFMLPSE
     AAVSMNLAEQ TRKVLATLTP REEKVLRMRF GIGEKADHTL EEVGQDFTVT RERIRQIEAK
     ALRKLRHPTR SRKLKSFIDN
//
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