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Database: UniProt
Entry: J7QNP3_METSZ
LinkDB: J7QNP3_METSZ
Original site: J7QNP3_METSZ 
ID   J7QNP3_METSZ            Unreviewed;       671 AA.
AC   J7QNP3;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-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   OrderedLocusNames=BN69_1557 {ECO:0000313|EMBL:CCJ07008.1};
OS   Methylocystis sp. (strain SC2).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylocystaceae; Methylocystis.
OX   NCBI_TaxID=187303 {ECO:0000313|EMBL:CCJ07008.1, ECO:0000313|Proteomes:UP000005263};
RN   [1] {ECO:0000313|EMBL:CCJ07008.1, ECO:0000313|Proteomes:UP000005263}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC2 {ECO:0000313|EMBL:CCJ07008.1,
RC   ECO:0000313|Proteomes:UP000005263};
RX   PubMed=23045511; DOI=10.1128/JB.01446-12;
RA   Dam B., Dam S., Kube M., Reinhardt R., Liesack W.;
RT   "Complete Genome Sequence of Methylocystis sp. Strain SC2, an Aerobic
RT   Methanotroph with High-Affinity Methane Oxidation Potential.";
RL   J. Bacteriol. 194:6008-6009(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; HE956757; CCJ07008.1; -; Genomic_DNA.
DR   RefSeq; WP_014891037.1; NC_018485.1.
DR   AlphaFoldDB; J7QNP3; -.
DR   STRING; 187303.BN69_1557; -.
DR   KEGG; msc:BN69_1557; -.
DR   PATRIC; fig|187303.17.peg.1694; -.
DR   eggNOG; COG0568; Bacteria.
DR   HOGENOM; CLU_014793_7_1_5; -.
DR   OrthoDB; 9809557at2; -.
DR   Proteomes; UP000005263; 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          461..474
FT                   /note="RNA polymerase sigma-70"
FT                   /evidence="ECO:0000259|PROSITE:PS00715"
FT   DOMAIN          630..656
FT                   /note="RNA polymerase sigma-70"
FT                   /evidence="ECO:0000259|PROSITE:PS00716"
FT   DNA_BIND        631..650
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          77..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          201..249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          437..507
FT                   /note="Sigma-70 factor domain-2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   REGION          516..592
FT                   /note="Sigma-70 factor domain-3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   REGION          605..658
FT                   /note="Sigma-70 factor domain-4"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   MOTIF           461..464
FT                   /note="Interaction with polymerase core subunit RpoC"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   COMPBIAS        79..102
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   671 AA;  75891 MW;  82BF15575D894554 CRC64;
     MAKKDETKVE NETVAATEAS DGPLLDLNDA AVKRMIKLAK KRGFVTYAEL NAVLPSEEVS
     SDQIEDVYAM LSEMGITVSE GDDPDDVEAD EQNPEEEEPE GGELVESPRA TAVATRTSEP
     ADRTDDPVRM YLREMGSVEL LSREGEIAIA KRIEAGREAM IAGLCESPLT FQAIIIWREE
     LEAGKVLLRD IIDLEATYAG PEGKAAKSAE PAPAADLAPA TAPRTPPAGL QEDVPPAEET
     FEEEDDMENS VSLSAMELEL KPKVLETFAR IADAYKKLRR LQDQNVENKL KNETLTPAQE
     RKYKTLKKEI VADVKSLSLN QNRIEALVEQ LYDINKRLIG YETKLLRLAD SHGVMREDFI
     DKFHGSELDP KWVMRVAKLG SKGWREFVAA DKDRIKDLRT EIHALATETG LEISEFRKIV
     HMVQKGEREA RQAKKEMVEA NLRLVISIAK KYTNRGLQFL DLIQEGNIGL MKAVDKFEYR
     RGYKFSTYAT WWIRQAITRS IADQARTIRI PVHMIETINK IVRTSRQMLH EIGREPTPEE
     LSEKLAMPLE KVRKVLKIAK EPISLETPIG DEEDSHLGDF IEDKNAVLPI EAAIQSNLRE
     TTTRVLSSLT PREERVLRMR FGIGMNTDHT LEEVGQQFSV TRERIRQIEA KALRKLKHPS
     RSRKLRSFLD N
//
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