ID C5EYF0_9HELI Unreviewed; 615 AA.
AC C5EYF0;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=RNA polymerase sigma factor SigA {ECO:0000256|HAMAP-Rule:MF_00963};
GN Name=rpoD {ECO:0000313|EMBL:EEQ62920.1};
GN Synonyms=sigA {ECO:0000256|HAMAP-Rule:MF_00963};
GN ORFNames=HPMG_00377 {ECO:0000313|EMBL:EEQ62920.1};
OS Helicobacter pullorum MIT 98-5489.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=537972 {ECO:0000313|EMBL:EEQ62920.1};
RN [1] {ECO:0000313|EMBL:EEQ62920.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MIT 98-5489 {ECO:0000313|EMBL:EEQ62920.1};
RG The Broad Institute Genome Sequencing Platform;
RA Fox J.G., Shen Z., Charoenlap N., Schauer D.B., Ward D., Mehta T.,
RA Young S., Jaffe D., Gnerre S., Berlin A., Heiman D., Hepburn T., Shea T.,
RA Sykes S., Alvarado L., Kodira C., Borodovsky M., Lander E., Galagan J.,
RA Nusbaum C., Birren B.;
RT "Annotation of Helicobacter pullorum strain MIT 98-5489.";
RL Submitted (AUG-2008) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00963}.
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DR EMBL; DS990441; EEQ62920.1; -; Genomic_DNA.
DR RefSeq; WP_005020987.1; NZ_DS990441.1.
DR AlphaFoldDB; C5EYF0; -.
DR GeneID; 57004618; -.
DR eggNOG; COG0568; Bacteria.
DR HOGENOM; CLU_014793_7_2_7; -.
DR Proteomes; UP000003953; 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 Gene3D; 1.10.601.10; RNA Polymerase Primary Sigma Factor; 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};
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 404..417
FT /note="RNA polymerase sigma-70"
FT /evidence="ECO:0000259|PROSITE:PS00715"
FT DOMAIN 574..600
FT /note="RNA polymerase sigma-70"
FT /evidence="ECO:0000259|PROSITE:PS00716"
FT DNA_BIND 575..594
FT /note="H-T-H motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT REGION 175..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..450
FT /note="Sigma-70 factor domain-2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT REGION 459..535
FT /note="Sigma-70 factor domain-3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT MOTIF 404..407
FT /note="Interaction with polymerase core subunit RpoC"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT COMPBIAS 175..193
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 615 AA; 71416 MW; 2910C263A116D61C CRC64;
MSAKNINQQL DELFQSSSKY VSYEKIAQVL IKLPTAAQAK RVTELAKKYN KQLMSASEVA
KLLNQDEARR IKEDKKRLLD EELEDEFDFM KERELLEWSR SDSPVRMYLR EMGQIPLLTR
EDEVELSKNI ELGENIILDA ICSVPYLIDF ILDYKEALIN RERRVKELFK SFDDEEDEES
VESEEEELEE GEEESEGKKP ISKKDQKRVE KVLVSFKALE KAKKDWLKTW EQEKGEENGD
MLYLLTLAHK KQFLKEKLLD LGPTSKLITE LVKAMENTIK SDEGFERELK RLEYRLPLFN
DILLANHKKI LDNIIEMSKS DIVAAVPEAT MVSTYMEIKK LFQTKVASEE SFDLEPEKLK
QILEQIKRGK DIADRAKTKM AKSNLRLVVS IAKRYTNRGL PFLDLIQEGN IGLMKAVDKF
EYKKGYKFST YATWWIRQAI SRAIADQART IRIPIHMIET INRINKIMRK YLQEEGKEPD
IEKIAEEVGL PVDKVKNVIK ITKEPISLEA PIGNGEDGKF GDFVEDKASL GPMDSILKED
LKAQIDDVLD QLNEREKAVI RMRFGLLDDE SDRTLEEIGK ELNVTRERVR QIESSAIKKL
KHPKVGRKLK NYIED
//
