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Database: UniProt
Entry: Q2NWE9_SODGM
LinkDB: Q2NWE9_SODGM
Original site: Q2NWE9_SODGM 
ID   Q2NWE9_SODGM            Unreviewed;       615 AA.
AC   Q2NWE9;
DT   07-FEB-2006, integrated into UniProtKB/TrEMBL.
DT   07-FEB-2006, sequence version 1.
DT   27-MAR-2024, entry version 123.
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:CRL43897.1};
GN   OrderedLocusNames=SG0251 {ECO:0000313|EMBL:BAE73526.1};
GN   ORFNames=SGGMMB4_00640 {ECO:0000313|EMBL:CRL43897.1};
OS   Sodalis glossinidius (strain morsitans).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Bruguierivoracaceae; Sodalis.
OX   NCBI_TaxID=343509 {ECO:0000313|EMBL:BAE73526.1, ECO:0000313|Proteomes:UP000001932};
RN   [1] {ECO:0000313|EMBL:BAE73526.1, ECO:0000313|Proteomes:UP000001932}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Morsitans {ECO:0000313|EMBL:BAE73526.1}, and morsitans
RC   {ECO:0000313|Proteomes:UP000001932};
RX   PubMed=16365377; DOI=10.1101/gr.4106106;
RA   Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K., Hattori M.,
RA   Aksoy S.;
RT   "Massive genome erosion and functional adaptations provide insights into
RT   the symbiotic lifestyle of Sodalis glossinidius in the tsetse host.";
RL   Genome Res. 16:149-156(2006).
RN   [2] {ECO:0000313|EMBL:CRL43897.1, ECO:0000313|Proteomes:UP000245838}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:CRL43897.1}, and morsitans
RC   {ECO:0000313|Proteomes:UP000245838};
RA   Goodhead I.;
RL   Submitted (MAY-2015) 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; AP008232; BAE73526.1; -; Genomic_DNA.
DR   EMBL; LN854557; CRL43897.1; -; Genomic_DNA.
DR   RefSeq; WP_011410115.1; NZ_LN854557.1.
DR   STRING; 343509.SG0251; -.
DR   KEGG; sgl:SG0251; -.
DR   eggNOG; COG0568; Bacteria.
DR   HOGENOM; CLU_014793_7_0_6; -.
DR   OrthoDB; 9809557at2; -.
DR   Proteomes; UP000001932; Chromosome.
DR   Proteomes; UP000245838; Chromosome sggmmb4_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; 1.10.220.120; 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   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          405..418
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          180..216
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          381..451
FT                   /note="Sigma-70 factor domain-2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   REGION          460..536
FT                   /note="Sigma-70 factor domain-3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   REGION          549..602
FT                   /note="Sigma-70 factor domain-4"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   MOTIF           405..408
FT                   /note="Interaction with polymerase core subunit RpoC"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   COMPBIAS        190..212
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   615 AA;  70379 MW;  1EDB0F2FE5041194 CRC64;
     MEQNPQSQLK LLVTRGKEQG YLTFAEVNDH LPEDIVDSDQ IEDIIQMIND MGIQVMEEAP
     DADDLLLAET TSDTDEDAAE AAAQVLSSVE SEIGRTTDPV RMYMREMGTV ELLTREGEID
     IAKRIEDGIN QVQCSVAEYP EAITYLLEQY DRVEAGEARL SDLITGFVDP NAEEDMAPTA
     THIGSELSAD EIADDDDEDE EDGDDDSTDD DNSIDPELAR QKFVELREQY EITRNVIKTN
     GRSHAKSASE ILNLSDVFKQ FRLVPKQFDY LVNNMRAMMD RVRTQERLIM KLCVEISKMP
     KKNFVTLFAG NETSESWFKA ALAMNKPWSE KLHEVDDDVY RSLQKLRQIE EETGLTIEQV
     KDINRRMSIG EAKARRAKKE MVEANLRLVI SIAKKYTNRG LQFLDLIQEG NIGLMKAVDK
     FEYRRGYKFS TYATWWIRQA ITRSIADQAR TIRIPVHMIE TINKLNRISR QMLQEMGREP
     TPEELAERML MPEDKIRKVL KIAKEPISME TPIGDDEDSH LGDFIEDTTL ELPLDSATSE
     SLRSATHDVL AGLTAREAKV LRMRFGIDMN TDHTLEEVGK QFDVTRERIR QIEAKALRKL
     RHPSRSEVLR SFLDD
//
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