ID B6INX9_RHOCS Unreviewed; 648 AA.
AC B6INX9;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 98.
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:ACI99399.1};
GN OrderedLocusNames=RC1_2006 {ECO:0000313|EMBL:ACI99399.1};
OS Rhodospirillum centenum (strain ATCC 51521 / SW).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Rhodospirillum.
OX NCBI_TaxID=414684 {ECO:0000313|EMBL:ACI99399.1, ECO:0000313|Proteomes:UP000001591};
RN [1] {ECO:0000313|Proteomes:UP000001591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51521 / SW {ECO:0000313|Proteomes:UP000001591};
RA Touchman J.W., Bauer C., Blankenship R.E.;
RT "Genome sequence of Rhodospirillum centenum.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACI99399.1, ECO:0000313|Proteomes:UP000001591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51521 / SW {ECO:0000313|Proteomes:UP000001591};
RX PubMed=20500872; DOI=10.1186/1471-2164-11-325;
RA Lu Y.K., Marden J., Han M., Swingley W.D., Mastrian S.D., Chowdhury S.R.,
RA Hao J., Helmy T., Kim S., Kurdoglu A.A., Matthies H.J., Rollo D.,
RA Stothard P., Blankenship R.E., Bauer C.E., Touchman J.W.;
RT "Metabolic flexibility revealed in the genome of the cyst-forming alpha-1
RT proteobacterium Rhodospirillum centenum.";
RL BMC Genomics 11:325-325(2010).
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; CP000613; ACI99399.1; -; Genomic_DNA.
DR RefSeq; WP_012567184.1; NC_011420.2.
DR AlphaFoldDB; B6INX9; -.
DR STRING; 414684.RC1_2006; -.
DR KEGG; rce:RC1_2006; -.
DR eggNOG; COG0568; Bacteria.
DR HOGENOM; CLU_014793_7_1_5; -.
DR OrthoDB; 9809557at2; -.
DR Proteomes; UP000001591; Chromosome.
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:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
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 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:ACI99399.1};
KW Nucleotidyltransferase {ECO:0000313|EMBL:ACI99399.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001591};
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}; Transferase {ECO:0000313|EMBL:ACI99399.1}.
FT DOMAIN 438..451
FT /note="RNA polymerase sigma-70"
FT /evidence="ECO:0000259|PROSITE:PS00715"
FT DOMAIN 607..633
FT /note="RNA polymerase sigma-70"
FT /evidence="ECO:0000259|PROSITE:PS00716"
FT DNA_BIND 608..627
FT /note="H-T-H motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 81..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..484
FT /note="Sigma-70 factor domain-2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT REGION 493..569
FT /note="Sigma-70 factor domain-3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT REGION 582..635
FT /note="Sigma-70 factor domain-4"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT MOTIF 438..441
FT /note="Interaction with polymerase core subunit RpoC"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT COMPBIAS 198..224
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 648 AA; 73421 MW; 4934264D6C6AD217 CRC64;
MATKATQSAE VTDTREDEAN GPLMDNMAIA VKKMIQRGKE RGYVTYDELN AALPPDQSSS
EQIEDTMAQL SEMGINVVEG EEPEDGQDAS GDGEGRVSGN LDDDDIGRTD DPVRMYLREM
GSVELLSREG EIAIAKRIEA GREMMIGAIC ESPLTIRAII EWHQSLMEGK MLLRDIIDLD
ATYGIDPESG EPTGEDLSAV EAESEEEETP ERPEGAEGEP EGGDEEGNIS LSAMEAELKP
KVIETFARIE ETYEKLHKVQ EQRLAVLQRG EELPKGSDKK YDKLKAELTD LVNSVRLNNA
RIEQLVEQLY GLNRKLLGYE GKLLRLATDC KIKREDFLHH YYGSELDPNW LERCRGLSKS
WGRFADKSSV EVGRVREAIS EVADQVRLPI GEFRRIVSTV QKGEKEASRA KKEMVEANLR
LVISIAKKYT NRGLQFLDLI QEGNIGLMKA VDKFEYRRGY KFSTYATWWI RQAITRSIAD
QARTIRIPVH MIETINKLVR TSRQMLHEIG REPTPEELAE RLMMPLEKVR KVLKIAKEPI
SLETPIGDEE DSHLGDFIED KNAVLPLDAA IQANLRETTT RILATLTPRE ERVLRMRFGI
GMNTDHTLEE VGQQFSVTRE RIRQIEAKAL RKLKHPSRSR KLRSFLDT
//
