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Database: UniProt
Entry: A0A0B5DYE2_9RHOB
LinkDB: A0A0B5DYE2_9RHOB
Original site: A0A0B5DYE2_9RHOB 
ID   A0A0B5DYE2_9RHOB        Unreviewed;       666 AA.
AC   A0A0B5DYE2;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 43.
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   ORFNames=P73_3314 {ECO:0000313|EMBL:AJE48029.1};
OS   Celeribacter indicus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Celeribacter.
OX   NCBI_TaxID=1208324 {ECO:0000313|EMBL:AJE48029.1, ECO:0000313|Proteomes:UP000031521};
RN   [1] {ECO:0000313|EMBL:AJE48029.1, ECO:0000313|Proteomes:UP000031521}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P73 {ECO:0000313|EMBL:AJE48029.1};
RX   PubMed=25256706; DOI=10.1099/ijs.0.069039-0;
RA   Lai Q., Cao J., Yuan J., Li F., Shao Z.;
RT   "Celeribacter indicus sp. nov., a polycyclic aromatic hydrocarbon-degrading
RT   bacterium from deep-sea sediment and reclassification of Huaishuia
RT   halophila as Celeribacter halophilus comb. nov.";
RL   Int. J. Syst. Evol. Microbiol. 64:4160-4167(2014).
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; CP004393; AJE48029.1; -; Genomic_DNA.
DR   RefSeq; WP_043870452.1; NZ_FNNW01000002.1.
DR   AlphaFoldDB; A0A0B5DYE2; -.
DR   STRING; 1208324.P73_3314; -.
DR   KEGG; cid:P73_3314; -.
DR   HOGENOM; CLU_014793_7_0_5; -.
DR   OrthoDB; 9809557at2; -.
DR   Proteomes; UP000031521; 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   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}; Reference proteome {ECO:0000313|Proteomes:UP000031521};
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          456..469
FT                   /note="RNA polymerase sigma-70"
FT                   /evidence="ECO:0000259|PROSITE:PS00715"
FT   DOMAIN          625..651
FT                   /note="RNA polymerase sigma-70"
FT                   /evidence="ECO:0000259|PROSITE:PS00716"
FT   DNA_BIND        626..645
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   REGION          80..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          210..242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          432..502
FT                   /note="Sigma-70 factor domain-2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   REGION          511..587
FT                   /note="Sigma-70 factor domain-3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   REGION          600..653
FT                   /note="Sigma-70 factor domain-4"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   COILED          411..438
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOTIF           456..459
FT                   /note="Interaction with polymerase core subunit RpoC"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   COMPBIAS        213..227
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        228..242
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   666 AA;  74939 MW;  85761328A6452A20 CRC64;
     MAAKDNDDTK TEDQDQDAML DVSQAAVKKM ISEAREKGYI TYDQLNKVLP PEQVSSEQIE
     DVMSMLSEMG INVIEDEEVE DEDGAVEGEA RPGGELVTTG GSRELATASG ETEKLDRTDD
     PVRMYLREMG SVELLSREGE IAIAKRIEAG RNTMIAGLCE SPLTFQAITI WHDELLSEDI
     LLRDVIDLEA TFGGGVEGDD EAGVVEGLAV ESGSGEAKEK EQEYDADGNP ISSDDDEDDD
     EQANMSLAAM EAALKPQVLE TLARISSDFA TLSEMQDLRM SATLNEDGSF SAANEADYQT
     LRGEIVALVN SLHLHNNRIE ALIDQLYGIN KRIMTIDSSM VKLADQARIN RKEFIDEYRG
     AELDPTWLDR MAGKAGRGWQ MFIERHSDKV EELRSEMAMV GQYVGVDISE FRRIVAQVQK
     GEKEARQAKK EMVEANLRLV ISIAKKYTNR GLQFLDLIQE GNIGLMKAVD KFEYRRGYKF
     STYATWWIRQ AITRSIADQA RTIRIPVHMI ETINKLVRTG RQMLHEIGRE PTPEELAEKL
     QMPLEKVRKV MKIAKEPISL ETPIGDEEDS QLGDFIEDKN AVLPLDAAIQ ENLKETTTRV
     LASLTPREER VLRMRFGIGM NTDHTLEEVG QQFSVTRERI RQIEAKALRK LKHPSRSRKL
     RSFLDQ
//
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