RPOD_BUCAI
ID RPOD_BUCAI Reviewed; 612 AA.
AC P57163;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 03-AUG-2022, entry version 123.
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}; OrderedLocusNames=BU055;
OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS pisum symbiotic bacterium).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=107806;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APS;
RX PubMed=10993077; DOI=10.1038/35024074;
RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT sp. APS.";
RL Nature 407:81-86(2000).
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; BA000003; BAB12778.1; -; Genomic_DNA.
DR RefSeq; NP_239892.1; NC_002528.1.
DR RefSeq; WP_009874012.1; NC_002528.1.
DR AlphaFoldDB; P57163; -.
DR SMR; P57163; -.
DR STRING; 107806.10038743; -.
DR EnsemblBacteria; BAB12778; BAB12778; BAB12778.
DR KEGG; buc:BU055; -.
DR PATRIC; fig|107806.10.peg.64; -.
DR eggNOG; COG0568; Bacteria.
DR HOGENOM; CLU_014793_7_2_6; -.
DR OMA; RDAKKEM; -.
DR Proteomes; UP000001806; 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 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; Reference proteome; Sigma factor; Transcription;
KW Transcription regulation.
FT CHAIN 1..612
FT /note="RNA polymerase sigma factor RpoD"
FT /id="PRO_0000093877"
FT DNA_BIND 572..591
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00963"
FT REGION 191..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..448
FT /note="Sigma-70 factor domain-2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00963"
FT REGION 457..533
FT /note="Sigma-70 factor domain-3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00963"
FT REGION 546..599
FT /note="Sigma-70 factor domain-4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00963"
FT MOTIF 402..405
FT /note="Interaction with polymerase core subunit RpoC"
FT COMPBIAS 191..205
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 612 AA; 71050 MW; 6BDD03CC2E1D112A CRC64;
MDQNPQSQLK LLVTHGKEQG YLTYSEVNDH LPEDIIDSEQ IDDIIQMIND MGIPVVEEAP
DADDLILNEI NTDTDEDAVE AATQVLSSVE SELGRTTDPV RMYMREMGTV ELLTREGEID
IAKRIEEGIN QVQCSVSEYP EAITYLLEQY DRVKTGQIRL SDIITGFVDP NAEEIFPPTA
IHIGSELLDE QQNNEEDEEN NQEDHEDDHS IDPELANEKF SELRIQYNNT NNTIKNKNRT
HKDSLLEIYN LSEVFKQFRL VPKQFDHLVN NMRHMMERVR KQERIIIKLC VEICKMPKKN
FIKIFPIKKI NYLWFIREQN TNQPWSENLK KVKEDVFISV KKLIKIEEET GLTIEQVKDI
NKRMSIGEAK ARRAKKEMVE ANLRLVISIA KKYTNRGLQF LDLIQEGNIG LMKAVDKFEY
RRGYKFSTYA TWWIRQAITR SIADQARTIR IPVHMIETIN KLNRISRQML QEIGREPTPE
ELSEKMLIPE DKIRKVLKIA KEPISMETPI GDDDDSHLGD FIEDTTLELP LDSATSESLR
SATHDVLSGL TAREAKVLRM RFGIDMNTDH TLEEVGKQFD VTRERIRQIE AKALRKLRHP
SRSEVLRSFL DD