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Database: UniProt
Entry: Q2T2N0_BURTA
LinkDB: Q2T2N0_BURTA
Original site: Q2T2N0_BURTA 
ID   Q2T2N0_BURTA            Unreviewed;       483 AA.
AC   Q2T2N0;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 108.
DE   RecName: Full=RNA polymerase sigma factor {ECO:0000256|RuleBase:RU362124};
GN   OrderedLocusNames=BTH_I0088 {ECO:0000313|EMBL:ABC38558.1};
OS   Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CCUG 48851 /
OS   CIP 106301 / E264).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=271848 {ECO:0000313|EMBL:ABC38558.1, ECO:0000313|Proteomes:UP000001930};
RN   [1] {ECO:0000313|EMBL:ABC38558.1, ECO:0000313|Proteomes:UP000001930}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264
RC   {ECO:0000313|Proteomes:UP000001930};
RX   PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA   Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA   DeShazer D.;
RT   "Bacterial genome adaptation to niches: divergence of the potential
RT   virulence genes in three Burkholderia species of different survival
RT   strategies.";
RL   BMC Genomics 6:174-174(2005).
CC   -!- FUNCTION: Sigma factors are initiation factors that promote the
CC       attachment of RNA polymerase to specific initiation sites and are then
CC       released. {ECO:0000256|RuleBase:RU362124}.
CC   -!- SIMILARITY: Belongs to the sigma-70 factor family.
CC       {ECO:0000256|RuleBase:RU362124}.
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DR   EMBL; CP000086; ABC38558.1; -; Genomic_DNA.
DR   RefSeq; WP_009908303.1; NZ_CP008785.1.
DR   AlphaFoldDB; Q2T2N0; -.
DR   KEGG; bte:BTH_I0088; -.
DR   HOGENOM; CLU_014793_3_2_4; -.
DR   Proteomes; UP000001930; Chromosome I.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0016987; F:sigma factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0006352; P:DNA-templated transcription initiation; IEA:InterPro.
DR   CDD; cd06171; Sigma70_r4; 1.
DR   Gene3D; 1.10.601.10; RNA Polymerase Primary Sigma Factor; 2.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2.
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; IPR013325; RNA_pol_sigma_r2.
DR   InterPro; IPR013324; RNA_pol_sigma_r3/r4-like.
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; 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   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU362124};
KW   Sigma factor {ECO:0000256|ARBA:ARBA00023082,
KW   ECO:0000256|RuleBase:RU362124};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|RuleBase:RU362124};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW   ECO:0000256|RuleBase:RU362124}.
FT   DOMAIN          271..284
FT                   /note="RNA polymerase sigma-70"
FT                   /evidence="ECO:0000259|PROSITE:PS00715"
FT   DOMAIN          440..466
FT                   /note="RNA polymerase sigma-70"
FT                   /evidence="ECO:0000259|PROSITE:PS00716"
FT   REGION          33..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..61
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   483 AA;  52786 MW;  D1814545481CF83C CRC64;
     MKVSEREVRY EQGIDRLLEL ACARDDTEYA ELADEFASAP SDTHAHAHDL GEPEFLDRHA
     SDESAGTGSF GDKPTRAAHA DADWHDGDVV DAQSSEPSDA TPDDTAVSTD PLALFVRRMH
     AVPLLTHAQE IALATEIEAG REQVLQALAE TLDLLELASL PDDPALGRAR AALQRARARG
     DEGARAFARA RKAAYAALAA HGWPSAEIDA MRRAMRRLPT PPEQGDAGAL PAFADGEARI
     SAATARMAEA NLRLVLSIAR KYASRGLDLA DLLQEGNLGL LRAIEKFEYR RGFKFSTYAT
     WWIRQAISRA IADRARTIRV PVHVGDEARR VRKVADRIER RSGARASLAE LSEATGLSAE
     RLRAVLMLPR EPRSLNAPLG DDDQAEFGDI VEDASTPSLF DALAQGQMCD VVTSLLKTMS
     AQEADILRRR FGIGGDEPWS YEQIAAQAGV SREQIRRIEK RALQTLRITA DACNARDFLD
     AQP
//
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