ID   RPOD_PSEPU              Reviewed;         614 AA.
AC   P52327;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=RNA polymerase sigma factor RpoD {ECO:0000255|HAMAP-Rule:MF_00963};
DE   AltName: Full=Sigma-70 {ECO:0000255|HAMAP-Rule:MF_00963};
GN   Name=rpoD {ECO:0000255|HAMAP-Rule:MF_00963};
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=G1 / ATCC 17453;
RX   PubMed=8566819; DOI=10.1016/0378-1119(95)00675-3;
RA   Fujita M., Hanaura Y., Amemura A.;
RT   "Analysis of the rpoD gene encoding the principal sigma factor of
RT   Pseudomonas putida.";
RL   Gene 167:93-98(1995).
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:0000255|HAMAP-Rule:MF_00963}.
CC   -!- SUBUNIT: Interacts transiently with the RNA polymerase catalytic core.
CC       {ECO:0000255|HAMAP-Rule:MF_00963}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00963}.
CC   -!- SIMILARITY: Belongs to the sigma-70 factor family. RpoD/SigA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00963}.
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DR   EMBL; D30045; BAA06281.1; -; Genomic_DNA.
DR   PIR; JC4551; JC4551.
DR   AlphaFoldDB; P52327; -.
DR   SMR; P52327; -.
DR   PRIDE; P52327; -.
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   Gene3D; 1.10.10.10; -; 2.
DR   Gene3D; 1.10.220.120; -; 1.
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   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; SSF88659; SSF88659; 2.
DR   SUPFAM; SSF88946; SSF88946; 1.
DR   TIGRFAMs; TIGR02393; RpoD_Cterm; 1.
DR   TIGRFAMs; TIGR02937; sigma70-ECF; 1.
DR   PROSITE; PS00715; SIGMA70_1; 1.
DR   PROSITE; PS00716; SIGMA70_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; DNA-binding; Sigma factor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..614
FT                   /note="RNA polymerase sigma factor RpoD"
FT                   /id="PRO_0000093907"
FT   DNA_BIND        574..593
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00963"
FT   REGION          168..245
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          380..450
FT                   /note="Sigma-70 factor domain-2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00963"
FT   REGION          459..535
FT                   /note="Sigma-70 factor domain-3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00963"
FT   REGION          548..601
FT                   /note="Sigma-70 factor domain-4"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00963"
FT   MOTIF           404..407
FT                   /note="Interaction with polymerase core subunit RpoC"
FT   COMPBIAS        193..207
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        214..230
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   614 AA;  69726 MW;  53A0902E55B95274 CRC64;
     MSGKAQQQSR IKELITRGRE QGYLTYAEVN DHLPEDISDP EQVEDIIRMI NDMGINVFES
     APDADALLLA EADTDEAAAE EAAAALAAVE TDIRRTTDPV RMYMREMGTV ELLTREGEIE
     IAKRIEEGIR EVMGAIAHFP GTVDYILGEY DRVNRGCRLS DVLSGYIDPD DNIAAPTEEV
     PIPGTKAAAA KEEADDDEEE SEGGDDEEEP KAALTRSSQP SVSVRYPSSF SDHQGPEEKR
     SYPQGKRRAL QALADLFMPI KLVPKQFEVL VERVRDALNR LRQQERAIMQ LCVRDARMPR
     ADFLRMFPSN ETDQTWSGDL AKRNTKWAAA LGEKDAAIVA CQQKLIDLET ETGLTVAEIK
     EINRRMSIGE AKARRAKKEM VEANLRLVIS IAKKYTNRGL QFLDLIQEGN IGLMKAVDKF
     EYRRGYKFST YATWWIRQAI TRSIADQART IRIPVHMIET INKLNRISRQ MLQEMGREPT
     PEELGERMEM PEDKIRKVLK IAKEPISMET PIGDDEDSHL GDFIEDSTMQ SPIYVATVES
     LKEATRDVLS GLTAREAKVL RMRFGIDMNT DHTLEEVGKQ FDVTRERIRQ IEAKAWRKLR
     HPTRSEHLRS FLDE