SIGA_STRCO
ID SIGA_STRCO Reviewed; 511 AA.
AC P18183; O50539;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=RNA polymerase principal sigma factor HrdB;
DE AltName: Full=RNA polymerase sigma factor SigA {ECO:0000255|HAMAP-Rule:MF_00963};
GN Name=hrdB; Synonyms=sigA; OrderedLocusNames=SCO5820; ORFNames=SC5B8.10;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A3(2) / NRRL B-16638;
RX PubMed=1840545; DOI=10.1016/0378-1119(91)90308-x;
RA Shiina T., Tanaka K., Takahashi H.;
RT "Sequence of hrdB, an essential gene encoding sigma-like transcription
RT factor of Streptomyces coelicolor A3(2): homology to principal sigma
RT factors.";
RL Gene 107:145-148(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 306-357.
RC STRAIN=A3(2) / NRRL B-16638;
RX PubMed=3194753; DOI=10.1126/science.3194753;
RA Tanaka K., Shiina T., Takahashi H.;
RT "Multiple principal sigma factor homologs in eubacteria: identification of
RT the 'rpoD box'.";
RL Science 242:1040-1042(1988).
RN [4]
RP FUNCTION AS A SIGMA FACTOR, AND STIMULATION BY RBPA.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=16629670; DOI=10.1111/j.1365-2958.2006.05116.x;
RA Newell K.V., Thomas D.P., Brekasis D., Paget M.S.;
RT "The RNA polymerase-binding protein RbpA confers basal levels of rifampicin
RT resistance on Streptomyces coelicolor.";
RL Mol. Microbiol. 60:687-696(2006).
RN [5]
RP INTERACTION WITH RBPA, AND SUBUNIT.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=23605043; DOI=10.1093/nar/gkt277;
RA Tabib-Salazar A., Liu B., Doughty P., Lewis R.A., Ghosh S., Parsy M.L.,
RA Simpson P.J., O'Dwyer K., Matthews S.J., Paget M.S.;
RT "The actinobacterial transcription factor RbpA binds to the principal sigma
RT subunit of RNA polymerase.";
RL Nucleic Acids Res. 41:5679-5691(2013).
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. Its activity is stimulated by RbpA.
CC {ECO:0000255|HAMAP-Rule:MF_00963, ECO:0000269|PubMed:16629670}.
CC -!- SUBUNIT: Homotrimer (Potential). interacts transiently with the RNA
CC polymerase core complex. Interacts with RNA polymerase-binding protein
CC RbpA via its sigma-2 region (residues 211-347) in a free form.
CC {ECO:0000269|PubMed:23605043, ECO:0000305}.
CC -!- SIMILARITY: Belongs to the sigma-70 factor family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA37175.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X52983; CAA37175.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL939125; CAA18518.1; -; Genomic_DNA.
DR EMBL; AJ003022; CAA05813.1; -; Genomic_DNA.
DR PIR; S11712; S11712.
DR PIR; T35194; T35194.
DR RefSeq; NP_629943.1; NC_003888.3.
DR RefSeq; WP_003973202.1; NZ_VNID01000007.1.
DR AlphaFoldDB; P18183; -.
DR SMR; P18183; -.
DR STRING; 100226.SCO5820; -.
DR GeneID; 1101262; -.
DR KEGG; sco:SCO5820; -.
DR PATRIC; fig|100226.15.peg.5915; -.
DR eggNOG; COG0568; Bacteria.
DR HOGENOM; CLU_014793_2_2_11; -.
DR InParanoid; P18183; -.
DR OMA; QIPVTKW; -.
DR PhylomeDB; P18183; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR GO; GO:0001108; F:bacterial-type RNA polymerase holo enzyme binding; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016987; F:sigma factor activity; IDA:UniProtKB.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.10.10; -; 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; 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; 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 1: Evidence at protein level;
KW DNA-binding; Reference proteome; Sigma factor; Transcription;
KW Transcription regulation.
FT CHAIN 1..511
FT /note="RNA polymerase principal sigma factor HrdB"
FT /id="PRO_0000093991"
FT DNA_BIND 472..491
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00963"
FT REGION 72..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..347
FT /note="Binds RNA polymerase-binding protein RbpA"
FT REGION 278..348
FT /note="Sigma-70 factor domain-2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00963"
FT REGION 357..433
FT /note="Sigma-70 factor domain-3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00963"
FT REGION 446..499
FT /note="Sigma-70 factor domain-4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00963"
FT MOTIF 302..305
FT /note="Interaction with polymerase core subunit RpoC"
FT COMPBIAS 134..154
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 100
FT /note="K -> N (in Ref. 1; CAA37175)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 511 AA; 55935 MW; CE286A8B3EE141A8 CRC64;
MSASTSRTLP PEIAESVSVM ALIERGKAEG QIAGDDVRRA FEADQIPATQ WKNVLRSLNQ
ILEEEGVTLM VSAAEPKRTR KSVAAKSPAK RTATKAVAAK PVTSRKATAP AAPAAPATEP
AAVEEEAPAK KAAAKKTTAK KATAKKTTAK KAAAKKTTAK KEDGELLEDE ATEEPKAATE
EPEGTENAGF VLSDEDEDDA PAQQVAAAGA TADPVKDYLK QIGKVPLLNA EQEVELAKRI
EAGLFAEDKL ANSDKLAPKL KRELEIIAED GRRAKNHLLE ANLRLVVSLA KRYTGRGMLF
LDLIQEGNLG LIRAVEKFDY TKGYKFSTYA TWWIRQAITR AMADQARTIR IPVHMVEVIN
KLARVQRQML QDLGREPTPE ELAKELDMTP EKVIEVQKYG REPISLHTPL GEDGDSEFGD
LIEDSEAVVP ADAVSFTLLQ EQLHSVLDTL SEREAGVVSM RFGLTDGQPK TLDEIGKVYG
VTRERIRQIE SKTMSKLRHP SRSQVLRDYL D
