ID A0A6M6JPC4_9PSEU Unreviewed; 465 AA.
AC A0A6M6JPC4;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 1.
DT 18-JUN-2025, entry version 19.
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=HOP40_28755 {ECO:0000313|EMBL:QJY49255.1};
OS Pseudonocardia broussonetiae.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=2736640 {ECO:0000313|EMBL:QJY49255.1, ECO:0000313|Proteomes:UP000505377};
RN [1] {ECO:0000313|EMBL:QJY49255.1, ECO:0000313|Proteomes:UP000505377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gen01 {ECO:0000313|EMBL:QJY49255.1,
RC ECO:0000313|Proteomes:UP000505377};
RA Mo P.;
RL Submitted (MAY-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}.
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DR EMBL; CP053564; QJY49255.1; -; Genomic_DNA.
DR RefSeq; WP_172164600.1; NZ_CP053564.1.
DR AlphaFoldDB; A0A6M6JPC4; -.
DR KEGG; pbro:HOP40_28755; -.
DR Proteomes; UP000505377; 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 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 FunFam; 1.10.601.10:FF:000003; RNA polymerase sigma factor SigA; 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; IPR050239; Sigma-70_RNA_pol_init_factors.
DR InterPro; IPR028630; Sigma70_RpoD.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR NCBIfam; NF004560; PRK05901.1-1; 1.
DR NCBIfam; NF004561; PRK05901.1-3; 1.
DR NCBIfam; NF005920; PRK07921.1; 1.
DR NCBIfam; TIGR02393; RpoD_Cterm; 1.
DR NCBIfam; TIGR02937; sigma70-ECF; 1.
DR PANTHER; PTHR30603:SF59; RNA POLYMERASE PRINCIPAL SIGMA FACTOR HRDA; 1.
DR PANTHER; PTHR30603; RNA POLYMERASE SIGMA FACTOR RPO; 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:UP000505377};
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 256..269
FT /note="RNA polymerase sigma-70"
FT /evidence="ECO:0000259|PROSITE:PS00715"
FT DOMAIN 425..451
FT /note="RNA polymerase sigma-70"
FT /evidence="ECO:0000259|PROSITE:PS00716"
FT DNA_BIND 426..445
FT /note="H-T-H motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT REGION 1..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..302
FT /note="Sigma-70 factor domain-2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT REGION 311..387
FT /note="Sigma-70 factor domain-3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT REGION 400..453
FT /note="Sigma-70 factor domain-4"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT MOTIF 256..259
FT /note="Interaction with polymerase core subunit RpoC"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT COMPBIAS 25..37
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..48
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..65
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..87
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..116
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 465 AA; 51441 MW; FE3F5650043650E9 CRC64;
MAAADSATRT EPTADQAAAP APARRAPRAK TAPKPRAPRT GTKAAPAKKA GDEPDLDGAD
VDGAELDGAP EGADLEEVEV DLDDAELVPD APAKGVQVPG KATDEDEDDE DDDDEPANTG
VNRRGPRERS STPTKSSDFV WDEEESEALR QARKDAELTA SADSVRAYLK QIGKVALLNA
EEEVELAKRI EAGLYAAERL RRAIDAGEKV SPQLRRDLRW IVRDGERAKN HLLEANLRLV
VSLAKRYTGR GMAFLDLIQE GNLGLIRAVE KFDYTKGYKF STYATWWIRQ AITRAMADQA
RTIRIPVHMV EVINKLGRIQ RELLQDLGRE PTPEELAKEM DITPEKVLEI QQYAREPISL
DQTIGDEGDS QLGDFIEDSE AVVAVDAVSF TLLQDQLQSV LATLSEREAG VVRLRFGLTD
GQPRTLDEIG QVYGVTRERI RQIESKTMSK LRHPSRSQVL RDYLD
//
