ID I3TVC8_TISMK Unreviewed; 697 AA.
AC I3TVC8;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 70.
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:AFK56716.1};
GN OrderedLocusNames=TMO_c0106 {ECO:0000313|EMBL:AFK56716.1};
OS Tistrella mobilis (strain KA081020-065).
OG Plasmid pTM3 {ECO:0000313|EMBL:AFK56716.1,
OG ECO:0000313|Proteomes:UP000005258}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Geminicoccales;
OC Geminicoccaceae; Tistrella.
OX NCBI_TaxID=1110502 {ECO:0000313|EMBL:AFK56716.1, ECO:0000313|Proteomes:UP000005258};
RN [1] {ECO:0000313|EMBL:AFK56716.1, ECO:0000313|Proteomes:UP000005258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KA081020-065 {ECO:0000313|Proteomes:UP000005258};
RC PLASMID=Plasmid pTM3 {ECO:0000313|Proteomes:UP000005258};
RX PubMed=22458477; DOI=10.1021/ja301735a;
RA Xu Y., Kersten R.D., Nam S.J., Lu L., Al-Suwailem A.M., Zheng H.,
RA Fenical W., Dorrestein P.C., Moore B.S., Qian P.Y.;
RT "Bacterial biosynthesis and maturation of the didemnin anti-cancer
RT agents.";
RL J. Am. Chem. Soc. 134:8625-8632(2012).
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; CP003239; AFK56716.1; -; Genomic_DNA.
DR RefSeq; WP_014747705.1; NC_017958.1.
DR AlphaFoldDB; I3TVC8; -.
DR KEGG; tmo:TMO_c0106; -.
DR PATRIC; fig|1110502.3.peg.4969; -.
DR HOGENOM; CLU_014793_7_1_5; -.
DR Proteomes; UP000005258; Plasmid pTM3.
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}; Plasmid {ECO:0000313|EMBL:AFK56716.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005258};
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 487..500
FT /note="RNA polymerase sigma-70"
FT /evidence="ECO:0000259|PROSITE:PS00715"
FT DOMAIN 656..682
FT /note="RNA polymerase sigma-70"
FT /evidence="ECO:0000259|PROSITE:PS00716"
FT DNA_BIND 657..676
FT /note="H-T-H motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 82..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..533
FT /note="Sigma-70 factor domain-2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT REGION 542..618
FT /note="Sigma-70 factor domain-3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT REGION 631..684
FT /note="Sigma-70 factor domain-4"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT MOTIF 487..490
FT /note="Interaction with polymerase core subunit RpoC"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT COMPBIAS 82..96
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..274
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 697 AA; 78008 MW; 68BF2BC12215A11A CRC64;
MAKKATTAVE AGEGREDTPD GPLVDSLEIT VKKMVARAKE RGYISYDELN KALPQDQLSS
EQIEDVMAML SEMGINVVEN DEEGEELGEN QSGDDEEEEF GGSHATSVEE EELGRTDDPV
RMYLREMGSI ELLSREGEIL LAKRIEAGRN TMIGAICESP LTFRAIVRWR DALAAGEAML
RDIIDLEASY GGDQPPMTDE DAEAEAAMLA GDRPAVEPAK PVVNGNGAAA APAAAAAARP
EGEVRKASDN EEDEEDETVR AADSEEEEDE EGDGASVSIS VMEAELTPVI LESFDKIVEA
WAKLEKLQAK RLEAALKGEE QTTQARSRFE AAKSDVIEMV RGLNFAQARI DLLVEELYLL
NRSLMSLEGQ LMRLAVGCRV KREDFLRLYS GQELAPNWFQ VVGAQNGKAW KTFLERHGEE
AADIREGISR LAREVGLPIN EFKRIVSNVQ RGEREASQAK KEMVEANLRL VISIAKKYTN
RGLQFLDLIQ EGNIGLMKAV DKFEYRRGYK FSTYATWWIR QAITRSIADQ ARTIRIPVHM
IETINKLVRT SRQMLHEIGR EPTPEELAEK LQMPLEKVRK VLKIAKEPIS LETPIGDEED
SHLGDFIEDK NAILPVDAAI HSNLKETTTR VLASLTAREE RVLRMRFGIG MNTDHTLEEV
GQQFSVTRER IRQIEAKALR KLKHPSRSRK LRSFLDH
//
