ID A0A7C9QW03_9PROT Unreviewed; 674 AA.
AC A0A7C9QW03;
DT 10-FEB-2021, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2021, sequence version 1.
DT 18-JUN-2025, entry version 16.
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:NFV80676.1};
GN ORFNames=G4223_11210 {ECO:0000313|EMBL:NFV80676.1};
OS Magnetospirillum aberrantis SpK.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Rhodospirillales; Rhodospirillaceae; Magnetospirillum.
OX NCBI_TaxID=908842 {ECO:0000313|EMBL:NFV80676.1, ECO:0000313|Proteomes:UP000480684};
RN [1] {ECO:0000313|EMBL:NFV80676.1, ECO:0000313|Proteomes:UP000480684}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SpK {ECO:0000313|EMBL:NFV80676.1,
RC ECO:0000313|Proteomes:UP000480684};
RA Dziuba M., Kuznetsov B., Mardanov A., Ravin N., Grouzdev D.;
RL Submitted (FEB-2020) 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:NFV80676.1}.
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DR EMBL; JAAIYP010000038; NFV80676.1; -; Genomic_DNA.
DR RefSeq; WP_163679366.1; NZ_JAAIYP010000038.1.
DR AlphaFoldDB; A0A7C9QW03; -.
DR Proteomes; UP000480684; 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:UP000480684};
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 464..477
FT /note="RNA polymerase sigma-70"
FT /evidence="ECO:0000259|PROSITE:PS00715"
FT DOMAIN 633..659
FT /note="RNA polymerase sigma-70"
FT /evidence="ECO:0000259|PROSITE:PS00716"
FT DNA_BIND 634..653
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 79..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..510
FT /note="Sigma-70 factor domain-2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT REGION 519..595
FT /note="Sigma-70 factor domain-3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT REGION 608..661
FT /note="Sigma-70 factor domain-4"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT MOTIF 464..467
FT /note="Interaction with polymerase core subunit RpoC"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT COMPBIAS 1..12
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..98
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..251
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 674 AA; 75329 MW; 7DB8530195DE660D CRC64;
MATKSQNTAE VNESQDENLD GPLLDTLGVA VKKMVARGRE RGYVTYDELN AALPPDEVSS
EQIEDTMAML SELGVNVVES EEGEEAAPAE AEGEEEAEGY SASGNVDEED LGRTDDPVRM
YLREMGSVEL LSREGEIAIA KRIEAGREMM IGGICESPLT IRAVVDWHDA LQQGRMLLRD
IIDLDATYGN GPGADMTEED LEREVAGDDV EPKVKEGAEE GEEAEEPEGA EGEEGAEGEG
EGEGEGEGDG EEAGISLAAM EAALMPQVLE TFEAIAATHS KMEKALKDRL AILSKGETVS
PAAEKKYAKL RDEMIRLMDG VHLNNARIEQ LVEQMNGLNK RLMMLEGRLL RLAESCRVKR
QDFLDSYFGN ELDPKWIEVV GVKTKQWKDF AEKHGREIGD IRAKIAIVSG ESGLPISEFR
RIVQTVQRGE REASKAKKEM IEANLRLVIS IAKKYTNRGL QFLDLIQEGN IGLMKAVDKF
EYRRGYKFST YATWWIRQAI TRSIADQART IRIPVHMIET INKLVRTSRQ MLHEIGREPT
PEELAEKLSM PLEKVRKVLK IAKEPISLET PIGDEEDSHL GDFIEDKNAV LPLDAAIQAN
LRETTTRVLA SLTPREERVL RMRFGIGMNT DHTLEEVGQQ FSVTRERIRQ IEAKALRKLK
HPSRSRKLRS FLDT
//
