ID A1A259_BIFAA Unreviewed; 479 AA.
AC A1A259;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE RecName: Full=RNA polymerase sigma factor SigA {ECO:0000256|HAMAP-Rule:MF_00963};
GN Name=hrdB {ECO:0000313|EMBL:BAF39792.1};
GN Synonyms=sigA {ECO:0000256|HAMAP-Rule:MF_00963};
GN OrderedLocusNames=BAD_1011 {ECO:0000313|EMBL:BAF39792.1};
OS Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 /
OS E194a).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=367928 {ECO:0000313|EMBL:BAF39792.1, ECO:0000313|Proteomes:UP000008702};
RN [1] {ECO:0000313|EMBL:BAF39792.1, ECO:0000313|Proteomes:UP000008702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15703 / DSM 20083 / NCTC 11814 / E194a
RC {ECO:0000313|Proteomes:UP000008702};
RA Suzuki T., Tsuda Y., Kanou N., Inoue T., Kumazaki K., Nagano S., Hirai S.,
RA Tanaka K., Watanabe K.;
RT "Bifidobacterium adolescentis complete genome sequence.";
RL Submitted (DEC-2006) 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; AP009256; BAF39792.1; -; Genomic_DNA.
DR AlphaFoldDB; A1A259; -.
DR STRING; 367928.BAD_1011; -.
DR PaxDb; 1680-BADO_1063; -.
DR KEGG; bad:BAD_1011; -.
DR HOGENOM; CLU_014793_2_0_11; -.
DR Proteomes; UP000008702; 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; 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:UP000008702};
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 269..282
FT /note="RNA polymerase sigma-70"
FT /evidence="ECO:0000259|PROSITE:PS00715"
FT DOMAIN 438..464
FT /note="RNA polymerase sigma-70"
FT /evidence="ECO:0000259|PROSITE:PS00716"
FT DNA_BIND 439..458
FT /note="H-T-H motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT REGION 1..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 245..315
FT /note="Sigma-70 factor domain-2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT REGION 324..400
FT /note="Sigma-70 factor domain-3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT REGION 413..466
FT /note="Sigma-70 factor domain-4"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT REGION 460..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 269..272
FT /note="Interaction with polymerase core subunit RpoC"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT COMPBIAS 12..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..132
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 479 AA; 54229 MW; 80E5B1A3BE5AA543 CRC64;
MVYASGGINR RISLATKETT VNTEQTDLTE KTTSGKKAST RKPAAKKSES SKTATKTSRK
TAAKKTSAAK KSKKAEEEEE NLIEQDAPED DPVEDADLDD FDDDLDDVDD EGEDDDLDED
NIDEDDDSEL EDDDEDKRKK PEEPKEKGAF VVRDDDDDDN LTPSGNPKRR VIAAGATADP
VKDYLKQIGR VNLLNAEQEV DLSERIEAGL YAQHLLDTES DKMDFKRRRE LKWAANDGKR
AKDHLLEANL RLVVSLAKRY TGRGMLFLDL IQEGNLGLIR AVEKFDWKKG FKFSTYATWW
IRQAITRAMA DQARTIRVPV HMVEVINKLS RVQRQMLQDL GREPTPDELA RELDMPVEKV
QEVQKYGREP ISLHTPLGED GDSEFGDLIE DTDAIAPSDA VAFSLLQEQF KQVLETLSPR
EAGVIKMRYG LEDGQPKTLD DIGRVYGVTR ERIRQIESKT MSKLRHPSRS QTLRDFLDQ
//
