ID A0A0P0SIH9_9PSEU Unreviewed; 456 AA.
AC A0A0P0SIH9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=AD017_01430 {ECO:0000313|EMBL:ALL84163.1};
OS Pseudonocardia sp. EC080619-01.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=1096856 {ECO:0000313|EMBL:ALL84163.1, ECO:0000313|Proteomes:UP000066228};
RN [1] {ECO:0000313|EMBL:ALL84163.1, ECO:0000313|Proteomes:UP000066228}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC080619-01 {ECO:0000313|EMBL:ALL84163.1,
RC ECO:0000313|Proteomes:UP000066228};
RX PubMed=26535611; DOI=10.1021/jacs.5b09794;
RA Van Arnam E.B., Sit C.S.;
RT "A Rebeccamycin Analog Provides Plasmid-Encoded Niche Defense.";
RL J. Am. Chem. Soc. 137:14272-14274(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}.
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DR EMBL; CP012184; ALL84163.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P0SIH9; -.
DR STRING; 1096856.AD017_01430; -.
DR KEGG; pecq:AD017_01430; -.
DR PATRIC; fig|1096856.3.peg.297; -.
DR Proteomes; UP000066228; Chromosome.
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; 1.20.120.1810; -; 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; 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; 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|HAMAP-Rule:MF_00963};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_00963}; Reference proteome {ECO:0000313|Proteomes:UP000066228};
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 247..260
FT /note="RNA polymerase sigma-70"
FT /evidence="ECO:0000259|PROSITE:PS00715"
FT DOMAIN 416..442
FT /note="RNA polymerase sigma-70"
FT /evidence="ECO:0000259|PROSITE:PS00716"
FT DNA_BIND 417..436
FT /note="H-T-H motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT REGION 1..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..293
FT /note="Sigma-70 factor domain-2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT REGION 302..378
FT /note="Sigma-70 factor domain-3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT REGION 391..444
FT /note="Sigma-70 factor domain-4"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT MOTIF 247..250
FT /note="Interaction with polymerase core subunit RpoC"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..107
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 456 AA; 50643 MW; 806274E15ED05E47 CRC64;
MEPTSGTAPR SRRTSAAGTT GAATAKKPAA RTRKPGTATK AAPGTGPKKP AAKKASTKKA
DGEDAELEDG DVEIEDGELE EADIEADIAE AAQEVDAEDA SDDDEDDDTN TGKNRVAPTT
RSSQQKSADF VWDEEESEAL RQARKDAELT ASADSVRAYL KQIGKVALLN AEEEVELAKR
IEAGLYGAER IRKLFESNDK LSPQMRRDLR WIVRDGERAK NHLLEANLRL VVSLAKRYTG
RGMAFLDLIQ EGNLGLIRAV EKFDYTKGYK FSTYATWWIR QAITRAMADQ ARTIRIPVHM
VEVINKLGRI QRELLQDLGR EPTPEELAKE MDITPEKVLE IQQYAREPIS LDQTIGDEGD
SQLGDFIEDS EAVVAVDAVS FTLLQDQLQS VLATLSEREA GVVRLRFGLT DGQPRTLDEI
GQVYGVTRER IRQIESKTMS KLRHPSRSQV LRDYLD
//
