ID A0A0G0JXG5_9BACT Unreviewed; 827 AA.
AC A0A0G0JXG5;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=RNA polymerase sigma factor SigA {ECO:0000256|HAMAP-Rule:MF_00963};
GN Name=sigA {ECO:0000256|HAMAP-Rule:MF_00963};
GN ORFNames=US49_C0003G0064 {ECO:0000313|EMBL:KKQ33036.1};
OS candidate division TM6 bacterium GW2011_GWF2_37_49.
OC Bacteria; Candidatus Dependentiae.
OX NCBI_TaxID=1619083 {ECO:0000313|EMBL:KKQ33036.1, ECO:0000313|Proteomes:UP000033926};
RN [1] {ECO:0000313|EMBL:KKQ33036.1, ECO:0000313|Proteomes:UP000033926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKQ33036.1}.
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DR EMBL; LBTE01000003; KKQ33036.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0JXG5; -.
DR PATRIC; fig|1619083.3.peg.641; -.
DR Proteomes; UP000033926; 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 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; IPR028630; Sigma70_RpoD.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR NCBIfam; TIGR02393; RpoD_Cterm; 1.
DR NCBIfam; TIGR02937; sigma70-ECF; 1.
DR PANTHER; PTHR30603; RNA POLYMERASE SIGMA FACTOR RPO; 1.
DR PANTHER; PTHR30603:SF47; RNA POLYMERASE SIGMA FACTOR SIGF, CHLOROPLASTIC; 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};
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 594..607
FT /note="RNA polymerase sigma-70"
FT /evidence="ECO:0000259|PROSITE:PS00715"
FT DOMAIN 763..789
FT /note="RNA polymerase sigma-70"
FT /evidence="ECO:0000259|PROSITE:PS00716"
FT DNA_BIND 764..783
FT /note="H-T-H motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..640
FT /note="Sigma-70 factor domain-2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT REGION 649..725
FT /note="Sigma-70 factor domain-3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT REGION 738..791
FT /note="Sigma-70 factor domain-4"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT COILED 490..517
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 594..597
FT /note="Interaction with polymerase core subunit RpoC"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT COMPBIAS 15..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 827 AA; 94658 MW; C0C6D314F8B28EDF CRC64;
MKKMIKKLKI NKKENKKMTK PGDKKKAQLQ KKVAKPVQSK LKKKAEKLVA KTLKKQQNLT
KSKNAKFVKK AKKFIAKAAT TRHALISKSS AKVKVKIIAK PYSVKIKSIA KPAKIEHKKA
LVETKDQVKV AEKIKVENPK NAKLLKTSAI ENKKTKNVVL SAHALNEKSK IAHVSNIKDS
IKDLGLDEVS LDDEDFVLIE AEESGATQVN SLKLLEKQVA ALIEKGKNEG VLSYEELLAF
TSKNKLGEED TNELVSMFEK ENIDFIMQDE LEGGLSEGGF FGEEESGALP AKKDLKASLE
SSEYVGLDDD FEHDKELERL KSFIEPSQLN DPVKLYLKEI GKIPLLNKTT EKVIADKIAE
GKKQSIDSIS QFPFVAKELV GFSERLERDP LFLKEIIQFS DFDEDNSPKF EEEKIRLLEH
LNKIKDLIEN EDKIYRSYRG QLESEAKKKE MFTKVDQNKK NVVKAITDIK YSNKLIRKFG
KRIEKLVFKI QERETEIKGL DEKLKFYKNL KKQTQDDINQ IAGFESSIRS SQKMIKKTEQ
EAGLQKEKIA SLYMQFALAQ KKDKEAKDDL ARANLRLVVN IAKKYINRGL HFLDLIQEGN
IGLLKAVEKF EFERGFKFST YATWWIRQAI TRAIADQSRT IRVPVHMVET LSKINKITRN
YIQEAGREPT YSELAKELNL EEKKIKNIIK ISKEPVSLET PVGDSDDTSL KDFIEDENEY
SPVDAVVNED LKEKVREVLK TLTPREEKVL KMRFGIDVAS EHTLEEVGKD FSVTRERIRQ
IEVKALRKLR HPSRSKRLVN FFEKGVEAPI RNLDSCLDDE DDVDDAE
//