ID A0A0S8EGR3_9GAMM Unreviewed; 324 AA.
AC A0A0S8EGR3;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 13-SEP-2023, entry version 31.
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=AMS22_16330 {ECO:0000313|EMBL:KPK47656.1};
OS Thiotrichales bacterium SG8_50.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales.
OX NCBI_TaxID=1703416 {ECO:0000313|EMBL:KPK47656.1, ECO:0000313|Proteomes:UP000051903};
RN [1] {ECO:0000313|EMBL:KPK47656.1, ECO:0000313|Proteomes:UP000051903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_50 {ECO:0000313|EMBL:KPK47656.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK47656.1}.
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DR EMBL; LJTW01000312; KPK47656.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8EGR3; -.
DR PATRIC; fig|1703416.3.peg.2674; -.
DR Proteomes; UP000051903; 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 115..128
FT /note="RNA polymerase sigma-70"
FT /evidence="ECO:0000259|PROSITE:PS00715"
FT DOMAIN 284..310
FT /note="RNA polymerase sigma-70"
FT /evidence="ECO:0000259|PROSITE:PS00716"
FT DNA_BIND 285..304
FT /note="H-T-H motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00959"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 53..86
FT /note="Sigma-70 factor domain-1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00959"
FT REGION 91..161
FT /note="Sigma-70 factor domain-2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00959"
FT REGION 171..246
FT /note="Sigma-70 factor domain-3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00959"
FT REGION 259..312
FT /note="Sigma-70 factor domain-4"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00959"
FT MOTIF 115..118
FT /note="Interaction with polymerase core subunit RpoC"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00959"
FT COMPBIAS 1..24
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 324 AA; 37105 MW; 52059881DBA6E050 CRC64;
MEAEDETEIS TSVVAEDSDS DEERTSESAE PAETARETET REYGSDSYYS QADATRLYLR
EIGFSPLLTA EEEVYFARRA QKGDGAARKR MIESNLRLVV KIARRYMNRG LSLLDLIEEG
NLGLIRAVEK FDPERGFRFS TYATWWIRQT IERGIMNQTR TIRLPVHVLK EINIYQRAAR
HLAQKLDHEP SPEEVAALLD KPVEDVKEML GLNERIASVD APLDDDPDRS LLDAIADDRT
PDPENMLQHD DLQQLIELWL NELSDKQREV VERRFGLSGR EISTLEEVGA DIGVTRERVR
QIQVEALKRL RVILEKAGYS VEST
//
