ID A0A7C9GQ99_9SPHN Unreviewed; 683 AA.
AC A0A7C9GQ99;
DT 10-FEB-2021, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2021, sequence version 1.
DT 18-JUN-2025, entry version 17.
DE RecName: Full=RNA polymerase sigma factor RpoD {ECO:0000256|HAMAP-Rule:MF_00963};
DE AltName: Full=Sigma-70 {ECO:0000256|HAMAP-Rule:MF_00963};
GN Name=rpoD {ECO:0000256|HAMAP-Rule:MF_00963,
GN ECO:0000313|EMBL:MQT16331.1};
GN ORFNames=F3168_03550 {ECO:0000313|EMBL:MQT16331.1};
OS Polymorphobacter fuscus.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Sphingomonadales; Sphingosinicellaceae; Polymorphobacter.
OX NCBI_TaxID=1439888 {ECO:0000313|EMBL:MQT16331.1, ECO:0000313|Proteomes:UP000481327};
RN [1] {ECO:0000313|EMBL:MQT16331.1, ECO:0000313|Proteomes:UP000481327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D40P {ECO:0000313|EMBL:MQT16331.1,
RC ECO:0000313|Proteomes:UP000481327};
RA Liu Z.;
RT "Polymorphobacter sp. isolated from a lake in China.";
RL Submitted (SEP-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:MQT16331.1}.
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DR EMBL; WIOL01000001; MQT16331.1; -; Genomic_DNA.
DR RefSeq; WP_152576739.1; NZ_JAATJI010000001.1.
DR AlphaFoldDB; A0A7C9GQ99; -.
DR OrthoDB; 9809557at2; -.
DR Proteomes; UP000481327; 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; 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; IPR007631; RNA_pol_sigma_70_non-ess.
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; PF04546; Sigma70_ner; 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:UP000481327};
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 473..486
FT /note="RNA polymerase sigma-70"
FT /evidence="ECO:0000259|PROSITE:PS00715"
FT DOMAIN 642..668
FT /note="RNA polymerase sigma-70"
FT /evidence="ECO:0000259|PROSITE:PS00716"
FT DNA_BIND 643..662
FT /note="H-T-H motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..519
FT /note="Sigma-70 factor domain-2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT REGION 528..604
FT /note="Sigma-70 factor domain-3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT REGION 617..670
FT /note="Sigma-70 factor domain-4"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT MOTIF 473..476
FT /note="Interaction with polymerase core subunit RpoC"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT COMPBIAS 79..103
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..240
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 683 AA; 76599 MW; E3A49CBAA706A3E5 CRC64;
MAKANVAAAS TDAKGEGNDA PLLDLNEASV KKLLARAKKR GYITYDELNE ALPQDQMSSE
QIEDVMAALS EMGINIIEND EPADDGAEAA RAEDDEDEPE PVEGDLGTAP AAAVVKAPLD
RTDDPVRMYL REMGAVELLS REGEIAIAKR IEAGRNTMIA GLCESPMTFT AMIEWSNALN
EGRMQLREIL DLEAMLAKDP AEAATDENGE PTEGSDLPTV QFKDDEEPAE EPAAPDEEDG
MTERRMRPDG KPAIPDDEEE DTTLSLAAME EVLKPAALEK FAEITATYKK FLKLQETRLT
ALGGNTAFPA ADERRYQKLR EELTRGVQSI HFNNSKIELL VDQLYTQNRR LLVLGGQMMK
LADKHKINRK SFIDEYTGNE LDDSWMGRVA GIDKKWAAFA NAETAPVETI RSEIANIAEA
TGVELGEFRR VTNMVQKGER EARIAKKEMV EANLRLVISI AKKYTNRGLQ FLDLIQEGNI
GLMKAVDKFE YRRGYKFSTY ATWWIRQAIT RSIADQARTI RIPVHMIETI NKLVRTSRQI
LHEIGREPTP EELAERLSMP LEKVRKVMKI AKEPISLETP IGDEEDSHLG DFIEDKNAVI
PVDAAIHANL KETVTRVLAS LTPREERVLR MRFGIGMNTD HTLEEVGQQF SVTRERIRQI
EAKALRKLKH PSRSRKMRSF LDV
//
