ID A0A068NHF7_9ACTO Unreviewed; 596 AA.
AC A0A068NHF7;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 41.
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=FB03_01400 {ECO:0000313|EMBL:AIE82150.1};
OS Actinotignum schaalii.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinotignum.
OX NCBI_TaxID=59505 {ECO:0000313|EMBL:AIE82150.1, ECO:0000313|Proteomes:UP000035032};
RN [1] {ECO:0000313|EMBL:AIE82150.1, ECO:0000313|Proteomes:UP000035032}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 27420 {ECO:0000313|EMBL:AIE82150.1,
RC ECO:0000313|Proteomes:UP000035032};
RX PubMed=25189588;
RA Kristiansen R., Dueholm M.S., Bank S., Nielsen P.H., Karst S.M.,
RA Cattoir V., Lienhard R., Grisold A.J., Olsen A.B., Reinhard M., Soby K.M.,
RA Christensen J.J., Prag J., Thomsen T.R.;
RT "Complete Genome Sequence of Actinobaculum schaalii Strain CCUG 27420.";
RL Genome Announc. 2:e00880-14(2014).
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; CP008802; AIE82150.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A068NHF7; -.
DR KEGG; asg:FB03_01400; -.
DR Proteomes; UP000035032; 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; 1.10.601.10; RNA Polymerase Primary Sigma Factor; 2.
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: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};
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 387..400
FT /note="RNA polymerase sigma-70"
FT /evidence="ECO:0000259|PROSITE:PS00715"
FT DOMAIN 556..582
FT /note="RNA polymerase sigma-70"
FT /evidence="ECO:0000259|PROSITE:PS00716"
FT DNA_BIND 557..576
FT /note="H-T-H motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT REGION 1..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..433
FT /note="Sigma-70 factor domain-2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT REGION 442..518
FT /note="Sigma-70 factor domain-3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT REGION 531..584
FT /note="Sigma-70 factor domain-4"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT MOTIF 387..390
FT /note="Interaction with polymerase core subunit RpoC"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT COMPBIAS 1..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..253
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 596 AA; 64354 MW; 17854D512F843E91 CRC64;
MATKSASAQE TAAVEKDTAV SASASGTKKK AASRSSSRTA SATSAATASE STTAAKKPAA
KKATATKATT TKKTATKKAT STAGESKVSE SKAASSASSA KKATTAKSAA TKSAASKSTA
AKKTSTKKAA AEAEAPETVA AATEASASTT EAKEEKPAAK KPATRKTAAK KTTSKAAESK
AASTSKKATS KRATAKQEEP EDPEEHEDLE DEDFDVDAED VDAEDLDDDL EDDEDDSEDA
EEEPEEEEDE ADKETDSAAK TGTTGRNSRG GFTVKDSDDS DEPAVRVHVA GATADPVKDY
LKQIGKVPLL NAAEEVELAK RIEAGLYAQH LLDQGNLDKE KDHAYIRELR IISRDGKHAK
NHLLEANLRL VVSLAKRYTG RGMLFLDLIQ EGNLGLVRAV EKFDYAKGYK FSTYATWWIR
QAITRAMADQ ARTIRIPVHM VEVINKLARV QRQMLQELGR EPTTEELAKE LDMTEEKVVE
VQKYGREPIS LHTPLGEDGD SEFGDLIEDS EAVVPADAVG FTLLQEQLHR VLDTLSEREA
GVVSMRFGLT DGQPKTLDEI GKVYGVTRER IRQIESKTMS KLRHPSRSQV LRDYLE
//