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Database: UniProt
Entry: A0A0G0JXG5_9BACT
LinkDB: A0A0G0JXG5_9BACT
Original site: A0A0G0JXG5_9BACT 
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
//
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