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Database: UniProt
Entry: A0A0D6PAG4_9PROT
LinkDB: A0A0D6PAG4_9PROT
Original site: A0A0D6PAG4_9PROT 
ID   A0A0D6PAG4_9PROT        Unreviewed;       638 AA.
AC   A0A0D6PAG4;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 43.
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   ORFNames=Aam_007_027 {ECO:0000313|EMBL:GAN78740.1};
OS   Acidocella aminolytica 101 = DSM 11237.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acidocella.
OX   NCBI_TaxID=1120923 {ECO:0000313|EMBL:GAN78740.1, ECO:0000313|Proteomes:UP000032668};
RN   [1] {ECO:0000313|EMBL:GAN78740.1, ECO:0000313|Proteomes:UP000032668}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=101 / DSM 11237 {ECO:0000313|Proteomes:UP000032668};
RA   Azuma Y., Higashiura N., Hirakawa H., Matsushita K.;
RT   "Whole genome sequence of Acidocella aminolytica 101 = DSM 11237.";
RL   Submitted (NOV-2012) 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:GAN78740.1}.
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DR   EMBL; BANC01000007; GAN78740.1; -; Genomic_DNA.
DR   RefSeq; WP_048877232.1; NZ_FQVJ01000008.1.
DR   AlphaFoldDB; A0A0D6PAG4; -.
DR   STRING; 1120923.SAMN02746095_01202; -.
DR   OrthoDB; 9809557at2; -.
DR   Proteomes; UP000032668; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
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; 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; 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; 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   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}; DNA-directed RNA polymerase {ECO:0000313|EMBL:GAN78740.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032668};
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          428..441
FT                   /note="RNA polymerase sigma-70"
FT                   /evidence="ECO:0000259|PROSITE:PS00715"
FT   DOMAIN          597..623
FT                   /note="RNA polymerase sigma-70"
FT                   /evidence="ECO:0000259|PROSITE:PS00716"
FT   DNA_BIND        598..617
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          79..114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          189..216
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          404..474
FT                   /note="Sigma-70 factor domain-2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   REGION          483..559
FT                   /note="Sigma-70 factor domain-3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   REGION          572..625
FT                   /note="Sigma-70 factor domain-4"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   COILED          270..318
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOTIF           428..431
FT                   /note="Interaction with polymerase core subunit RpoC"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   COMPBIAS        85..99
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        195..215
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   638 AA;  72519 MW;  BDE70903FF2734C5 CRC64;
     MATKPTATTE TAAPEAEADA NVLDTQSGAV KRLIAKGKER GYITFDELNA VLPAEQNSSE
     QIEDIMAMLN EMGIQVVESE ENEEAETAAA PKEEANEEEE QAGNVSEASV SRTDDPVRMY
     LREMGTVELL SREGEIAIAK RIEAGRDMMI RGLCESPLTF RAIIAWHEAL NNGRVLLRDV
     IDLEAMQNGA EPTDDSFENE NENNEELDED EDGEGAGMSL SALEEKLKPE IFQNFDEIEK
     LYDKLSKMQT KRIETLTAGE DVNARNEKAY EKLRDELVAK VEQVRLHNNR IEELVAQLKV
     LNQRLNGLEG QLLRLAESTK VSRDDFLAHY RGNEMDPNWL AQMAELPGKG WKEFVRKHET
     QANELRTQIG RVASEAGLPI EEFRRVYMTV SRGERDSTRA KKEMIEANLR LVISIAKKYT
     NRGLQFLDLI QEGNIGLMKA VDKFEYRRGY KFSTYATWWI RQAITRSIAD QARTIRIPVH
     MIETINKLVR TSRQMLHEIG REPTPEELAE KLGMPLEKVR KVLKIAKEPI SLETPIGDEE
     DSHLGDFIED KAAIIPLDAA VHANLREAAT RVLSSLTPRE ERVLRMRFGI GMNTDHTLEE
     VGQQFNVTRE RIRQIEAKAL RKLKHPSRSR KLRSFLDD
//
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