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Database: UniProt
Entry: P77833_BORPT
LinkDB: P77833_BORPT
Original site: P77833_BORPT 
ID   P77833_BORPT            Unreviewed;       733 AA.
AC   P77833;
DT   01-FEB-1997, integrated into UniProtKB/TrEMBL.
DT   01-FEB-1997, sequence version 1.
DT   27-MAR-2024, entry version 127.
DE   RecName: Full=RNA polymerase sigma factor RpoD {ECO:0000256|HAMAP-Rule:MF_00963};
DE   AltName: Full=Sigma-70 {ECO:0000256|HAMAP-Rule:MF_00963};
GN   Name=rpoD {ECO:0000256|HAMAP-Rule:MF_00963,
GN   ECO:0000313|EMBL:AAC45085.1};
GN   ORFNames=NCTC10911_02460 {ECO:0000313|EMBL:SUV65410.1};
OS   Bordetella pertussis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=520 {ECO:0000313|EMBL:AAC45085.1};
RN   [1] {ECO:0000313|EMBL:AAC45085.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=18323 {ECO:0000313|EMBL:AAC45085.1};
RX   PubMed=9076731; DOI=10.1046/j.1365-2958.1997.2741639.x;
RA   Steffen P., Goyard S., Ullmann A.;
RT   "The Bordetella pertussis sigma subunit of RNA polymerase confers enhanced
RT   expression of fha in Escherichia coli.";
RL   Mol. Microbiol. 23:945-954(1997).
RN   [2] {ECO:0000313|EMBL:SUV65410.1, ECO:0000313|Proteomes:UP000255014}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC10911 {ECO:0000313|EMBL:SUV65410.1,
RC   ECO:0000313|Proteomes:UP000255014};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-2018) 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; U73858; AAC45085.1; -; Genomic_DNA.
DR   EMBL; UFTT01000002; SUV65410.1; -; Genomic_DNA.
DR   AlphaFoldDB; P77833; -.
DR   PATRIC; fig|520.334.peg.2385; -.
DR   Proteomes; UP000255014; 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; 1.10.220.120; Sigma-70 factor, region 1.1; 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; IPR007631; RNA_pol_sigma_70_non-ess.
DR   InterPro; IPR007127; RNA_pol_sigma_70_r1_1.
DR   InterPro; IPR042189; RNA_pol_sigma_70_r1_1_sf.
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; PF04546; Sigma70_ner; 1.
DR   Pfam; PF03979; Sigma70_r1_1; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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          522..535
FT                   /note="RNA polymerase sigma-70"
FT                   /evidence="ECO:0000259|PROSITE:PS00715"
FT   DOMAIN          691..717
FT                   /note="RNA polymerase sigma-70"
FT                   /evidence="ECO:0000259|PROSITE:PS00716"
FT   DNA_BIND        692..711
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   REGION          1..128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          298..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          498..568
FT                   /note="Sigma-70 factor domain-2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   REGION          577..653
FT                   /note="Sigma-70 factor domain-3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   REGION          666..719
FT                   /note="Sigma-70 factor domain-4"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   COILED          477..504
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOTIF           522..525
FT                   /note="Interaction with polymerase core subunit RpoC"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   COMPBIAS        41..58
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        94..128
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        298..319
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   733 AA;  81348 MW;  B18730BC7461F703 CRC64;
     MAAEKAPAKT AVKVAKPAAK TAAKKTATKT VAAKTAAADK PAKTTKARAK KAEDKLADLV
     GAARPAPSGR RPGRPAKNAN NDSDAFDDSM DGEGEVLPDL KPPKRGGKRG KADPKDLIAR
     GPVSPEEYEA RRNRLKQLIK LGKDRGYLTY GEINDHLPDD LVDAEAIDGI ISTFSDMGIA
     VYDQAPDAET LLMSENAPVA SNDDDVEDEA EAALTTVDSD FGRTTDPVRM YMREMGSVEL
     LTREGEIEIA KRIEDGLKHM VMAISACPTT INEILAHITR VREGQAQIDE VVDGLVDPED
     GEEYAGAGVT ADEDEGDDGP AGGMSSKQLE DLRVKALAKF DEVSKQFEKM RQSYEKEGYK
     SDAYLKAQDI IQTELMGIRF TAKMVEKLAD TLRAQVEEVR QLERAVLHTC VDRAGMPRSH
     FLKAFPGNET NLQWVLDEVA AAHAYSETLE RQIPAVQELQ QKLIDLQTRV VLPLKDLKDV
     NKRMATGEAK ARKAKREMTE ANLRLVISIA KKYTNRGLQF LDLIQEGNIG LMKAVDKFEY
     RRGYKFSTYA TWWIRQAITR SIADQARTIR IPVHMIETIN KMNRISRQIL QETGAEPDPA
     TLAQKMDMPE DKIRKILKIA KEPISMETPI GDDDDSHLGD FIEDTATLAP SDAALHGSMR
     DVVKEVLDSL TPREAKVLRM RFGIEMSTDQ TLEEVGKQFD VTRERIRQIE AKALRKLRHP
     SRADKLKSFL EGQ
//
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