ID A0A1Y2ZX54_9GAMM Unreviewed; 339 AA.
AC A0A1Y2ZX54;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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 ORFNames=BCS42_00245 {ECO:0000313|EMBL:OTE96472.1};
OS Crenothrix sp. D3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Crenotrichaceae; Crenothrix.
OX NCBI_TaxID=1880899 {ECO:0000313|EMBL:OTE96472.1, ECO:0000313|Proteomes:UP000198219};
RN [1] {ECO:0000313|EMBL:OTE96472.1, ECO:0000313|Proteomes:UP000198219}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D3 {ECO:0000313|EMBL:OTE96472.1};
RA Oswald K., Graf J.S., Littman S., Tienken D., Brand A., Wehrli B.,
RA Albertsen M., Daims H., Wagner M., Kuypers M.M., Schubert C.J., Milucka J.;
RT "Crenothrix are major methane consumers in stratified lakes.";
RL ISME J. 0:0-0(2017).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OTE96472.1}.
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DR EMBL; MBQZ01000036; OTE96472.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2ZX54; -.
DR STRING; 1880899.BCS42_00245; -.
DR Proteomes; UP000198219; Unassembled WGS sequence.
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};
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 128..141
FT /note="RNA polymerase sigma-70"
FT /evidence="ECO:0000259|PROSITE:PS00715"
FT DOMAIN 297..323
FT /note="RNA polymerase sigma-70"
FT /evidence="ECO:0000259|PROSITE:PS00716"
FT DNA_BIND 298..317
FT /note="H-T-H motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00959"
FT REGION 66..99
FT /note="Sigma-70 factor domain-1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00959"
FT REGION 104..174
FT /note="Sigma-70 factor domain-2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00959"
FT REGION 184..259
FT /note="Sigma-70 factor domain-3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00959"
FT REGION 272..325
FT /note="Sigma-70 factor domain-4"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00959"
FT MOTIF 128..131
FT /note="Interaction with polymerase core subunit RpoC"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00959"
SQ SEQUENCE 339 AA; 39058 MW; CD6E9BCBA2FF2587 CRC64;
MIEELIEPSD DDIVMVLDDD LSLDGEFDAA TAIIEKLRGD SYNPVDNNDD NEDIAVIKTR
SSADFDATRA YLNELSRSQL LTAEQERHYG KKALQGDQPA RKVMIESNLR LVVKIARRYL
NRGLPLLDLI EEGNLGLIRA VEKFDPDKGF RFSTYATWWI RQTIERALMN QTRTIRLPIH
IVKEMNIYLK AQRHLVNTLD YDPTALEIAE YLDKPVSKVE KMLKLNERVT SVDVPSGKDY
DKPLVDSLAD EASKTHEDRI QERDIKQNIT GWVFELPEKQ REVICRRYGL CGYPESTLEQ
VAQELGVTRE RVRQIQMDGL RQLKEILASH GYSFEAIFN
//
