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Database: UniProt
Entry: B8GRG7_THISH
LinkDB: B8GRG7_THISH
Original site: B8GRG7_THISH 
ID   B8GRG7_THISH            Unreviewed;       344 AA.
AC   B8GRG7;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   RecName: Full=RNA polymerase sigma factor RpoS {ECO:0000256|HAMAP-Rule:MF_00959};
DE   AltName: Full=Sigma S {ECO:0000256|HAMAP-Rule:MF_00959};
DE   AltName: Full=Sigma-38 {ECO:0000256|HAMAP-Rule:MF_00959};
GN   Name=rpoS {ECO:0000256|HAMAP-Rule:MF_00959};
GN   OrderedLocusNames=Tgr7_1436 {ECO:0000313|EMBL:ACL72521.1};
OS   Thioalkalivibrio sulfidiphilus (strain HL-EbGR7).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Thioalkalivibrio.
OX   NCBI_TaxID=396588 {ECO:0000313|EMBL:ACL72521.1, ECO:0000313|Proteomes:UP000002383};
RN   [1] {ECO:0000313|EMBL:ACL72521.1, ECO:0000313|Proteomes:UP000002383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HL-EbGR7 {ECO:0000313|EMBL:ACL72521.1,
RC   ECO:0000313|Proteomes:UP000002383};
RX   PubMed=21475584;
RA   Muyzer G., Sorokin D.Y., Mavromatis K., Lapidus A., Clum A., Ivanova N.,
RA   Pati A., d'Haeseleer P., Woyke T., Kyrpides N.C.;
RT   "Complete genome sequence of 'Thioalkalivibrio sulfidophilus' HL-EbGr7.";
RL   Stand. Genomic Sci. 4:23-35(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 master transcriptional regulator of
CC       the stationary phase and the general stress response.
CC       {ECO:0000256|HAMAP-Rule:MF_00959}.
CC   -!- SUBUNIT: Interacts with the RNA polymerase core enzyme.
CC       {ECO:0000256|HAMAP-Rule:MF_00959}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00959}.
CC   -!- SIMILARITY: Belongs to the sigma-70 factor family. RpoS subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00959}.
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DR   EMBL; CP001339; ACL72521.1; -; Genomic_DNA.
DR   RefSeq; WP_012638004.1; NC_011901.1.
DR   AlphaFoldDB; B8GRG7; -.
DR   STRING; 396588.Tgr7_1436; -.
DR   KEGG; tgr:Tgr7_1436; -.
DR   eggNOG; COG0568; Bacteria.
DR   HOGENOM; CLU_014793_3_5_6; -.
DR   OrthoDB; 9809557at2; -.
DR   Proteomes; UP000002383; 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; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2.
DR   HAMAP; MF_00959; Sigma70_RpoS; 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; IPR012761; RNA_pol_sigma_RpoS.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   NCBIfam; TIGR02394; rpoS_proteo; 1.
DR   NCBIfam; TIGR02937; sigma70-ECF; 1.
DR   PANTHER; PTHR30603; RNA POLYMERASE SIGMA FACTOR RPO; 1.
DR   PANTHER; PTHR30603:SF67; RNA POLYMERASE SIGMA FACTOR RPOS; 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|HAMAP-Rule:MF_00959};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00959}; Reference proteome {ECO:0000313|Proteomes:UP000002383};
KW   Sigma factor {ECO:0000256|ARBA:ARBA00023082, ECO:0000256|HAMAP-
KW   Rule:MF_00959};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW   Rule:MF_00959};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015, ECO:0000256|HAMAP-
KW   Rule:MF_00959}.
FT   DOMAIN          132..145
FT                   /note="RNA polymerase sigma-70"
FT                   /evidence="ECO:0000259|PROSITE:PS00715"
FT   DOMAIN          301..327
FT                   /note="RNA polymerase sigma-70"
FT                   /evidence="ECO:0000259|PROSITE:PS00716"
FT   DNA_BIND        302..321
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00959"
FT   REGION          1..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          70..103
FT                   /note="Sigma-70 factor domain-1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00959"
FT   REGION          108..178
FT                   /note="Sigma-70 factor domain-2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00959"
FT   REGION          188..263
FT                   /note="Sigma-70 factor domain-3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00959"
FT   REGION          276..329
FT                   /note="Sigma-70 factor domain-4"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00959"
FT   MOTIF           132..135
FT                   /note="Interaction with polymerase core subunit RpoC"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00959"
FT   COMPBIAS        1..25
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..54
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   344 AA;  39637 MW;  D0965EBA6A8F8643 CRC64;
     MPKRRRTEPP AGELEDEIRE DKLEAPDELG DEDEALVLAD ETEDVDEEEE DEDPATKVYA
     AGDVPKGELD ATRLYLSEIE FSPLLTPEEE VHYARLAQKG DEAGRRKMIE CNLRLVVKIA
     RRYMNRGLAL LDLIEEGNLG LIRAVEKFDP ERGFRFSTYA TWWIRQTIER ALMNQTRTIR
     LPIHVIKELN VYLRTARKLA QELDHEPTAE EVARHLDRPV GDVKRILALS ERVTSVDLPI
     GKDGERALLD VIPDEQTPEP SILIQDEDVV QFVDEWLQEL DEKQREVIVR RFGLHGYERS
     TLEQVGAELG VTRERVRQIQ MDALKRLRKI LESRGFSEEA LLQG
//
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