ID G2M788_HELPX Unreviewed; 672 AA.
AC G2M788;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
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=HPPN135_00445 {ECO:0000313|EMBL:AEN17803.1};
OS Helicobacter pylori Puno135.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1055529 {ECO:0000313|EMBL:AEN17803.1, ECO:0000313|Proteomes:UP000008533};
RN [1] {ECO:0000313|EMBL:AEN17803.1, ECO:0000313|Proteomes:UP000008533}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Puno135 {ECO:0000313|EMBL:AEN17803.1,
RC ECO:0000313|Proteomes:UP000008533};
RA Kersulyte D., Cabrera L., Hooper C.C., Jahuira Arias H., Gilman R.H.,
RA Berg D.E.;
RL Submitted (AUG-2011) 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; CP002982; AEN17803.1; -; Genomic_DNA.
DR AlphaFoldDB; G2M788; -.
DR KEGG; heu:HPPN135_00445; -.
DR PATRIC; fig|1055529.4.peg.86; -.
DR HOGENOM; CLU_014793_7_2_7; -.
DR Proteomes; UP000008533; 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; 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 461..474
FT /note="RNA polymerase sigma-70"
FT /evidence="ECO:0000259|PROSITE:PS00715"
FT DOMAIN 631..657
FT /note="RNA polymerase sigma-70"
FT /evidence="ECO:0000259|PROSITE:PS00716"
FT DNA_BIND 632..651
FT /note="H-T-H motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..507
FT /note="Sigma-70 factor domain-2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT REGION 516..592
FT /note="Sigma-70 factor domain-3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT MOTIF 461..464
FT /note="Interaction with polymerase core subunit RpoC"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
SQ SEQUENCE 672 AA; 77750 MW; 845317F433B00E08 CRC64;
MKKKANEEKA PKKAKAEAAQ ENKTKENNKA KESKIKEAKT KESKIKETKA KEPVPVKKLS
FNEALEELFA NSLSDCVSYE SIIQISAKVP TLAQVKKIKE LCQKYQKKLV SSSEYAKKLN
AIDKIKKTEE KQKVLDEELE DGYDFLKEKD FLEWSRSDSP VRMYLREMGD IKLLSKDEEI
ELSKQIRLGE DIILDAICSV PYLIDFIYAY KDALINRERR VKELFRSFDD DDENSVSDSK
KDDDSEEDEE NEERKKVVSE KDRKRVEKVQ ESFKALDKAK KEWLKALEAP VDEKEDELVR
LLTLAYKRQT LKDRLYDLEP TSKLINELVK TMETTLKSGD GFEKELKRLE YKLPLFNDAL
IANHKKILAN ITNMTKEDII AQVPEATMVS VYMDLKKLFL TKEASEEGFD LDPNKLKEIL
EQIKRGKLIS DRAKNKMAKS NLRLVVSIAK RFTSRGLPFL DLIQEGNIGL MKAVDKFEHE
KGFKFSTYAT WWIKQAISRA IADQARTIRI PIHMIDTINR INKVMRKHIQ ETGKEPDLEV
VAEEVGLSLD KVKNVIKVTK EPISLETPVG NDDDGKFGDF VEDKNIVSSI DHIMREDLKA
QIESVLDQLN EREKAVIRMR FGLLDDESDR TLEEIGKELN VTRERVRQIE SSAIKKLRSP
QYGRILRNYL RI
//
