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Database: UniProt
Entry: F4N2U7_YEREN
LinkDB: F4N2U7_YEREN
Original site: F4N2U7_YEREN 
ID   F4N2U7_YEREN            Unreviewed;       553 AA.
AC   F4N2U7;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
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:CBX72405.1};
GN   ORFNames=YEW_HH31370 {ECO:0000313|EMBL:CBX72405.1};
OS   Yersinia enterocolitica W22703.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=913028 {ECO:0000313|EMBL:CBX72405.1};
RN   [1] {ECO:0000313|EMBL:CBX72405.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=21453472; DOI=10.1186/1471-2164-12-168;
RA   Fuchs T.M., Brandt K., Starke M., Rattei T.;
RT   "Shotgun sequencing of Yersinia enterocolitica strain W22703 (biotype 2,
RT   serotype O:9): genomic evidence for oscillation between invertebrates and
RT   mammals.";
RL   BMC Genomics 12:168-168(2011).
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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00963}.
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DR   EMBL; FR718690; CBX72405.1; -; Genomic_DNA.
DR   AlphaFoldDB; F4N2U7; -.
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; 1.10.601.10; 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; 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; 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; IPR028630; Sigma70_RpoD.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
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   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; 1.
DR   PROSITE; PS00715; SIGMA70_1; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00963};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00963};
KW   Sigma factor {ECO:0000256|ARBA:ARBA00023082, ECO:0000256|HAMAP-
KW   Rule:MF_00963}; Transcription {ECO:0000256|HAMAP-Rule:MF_00963};
KW   Transcription regulation {ECO:0000256|HAMAP-Rule:MF_00963}.
FT   DOMAIN          445..458
FT                   /note="RNA polymerase sigma-70"
FT                   /evidence="ECO:0000259|PROSITE:PS00715"
FT   REGION          214..257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          421..491
FT                   /note="Sigma-70 factor domain-2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   MOTIF           445..448
FT                   /note="Interaction with polymerase core subunit RpoC"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   COMPBIAS        232..254
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   553 AA;  63324 MW;  DA17D4BFD349E93D CRC64;
     MWGQIPQYAV MAGSGDKKKP QMLLLAVSPT DTNPNTLKCG YRLMEQNPQS QLKLLVTRGK
     EQGYLTYAEV NDHLPEDIVD SDQIEDIIQM INDMGIQVLE EAPDADDLML AENTTDTDDD
     AAEAAAQVLS SVESEIGRTT DPVRMYMREM GTVELLTREG EIDIAKRIED GINQVQCSVA
     EYPEAITYLL EQYDRVEAGE ARLSDLITGF VDPNAEEDIA PTATHVGSEL STEEMDDDDD
     EDEDDEEEED DNSIDPELAR QKFSELREQY ENARLEIKKN GRSHANAAAE ILKLSEVFKQ
     FRLVPKQFDY LVNNMRAMMD RVRTQERIIM KLCVEQCKMP KKNFVTLFAS NETSDTWFAA
     AIAMGKPWSE KLKDVSDDVQ RSLQKLRQIE EETGLTIEQV KDINRRMSIG EAKARRAKKE
     MVEANLRLVI SIAKKYTNRG LQFLDLIQEG NIGLMKAVDK FEYRRGYKFS TYATWWIRQA
     ITRSIADQAR TIRIPVHMIE TINKLNRISR QMLQEMGREP TPEELAERML MPEDKIRKVL
     KIAKEPISME PNR
//
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