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Database: UniProt
Entry: A0A348HGN9_9GAMM
LinkDB: A0A348HGN9_9GAMM
Original site: A0A348HGN9_9GAMM 
ID   A0A348HGN9_9GAMM        Unreviewed;       351 AA.
AC   A0A348HGN9;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
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=ZBT109_2045 {ECO:0000313|EMBL:BBG30791.1};
OS   Zymobacter palmae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Zymobacter group; Zymobacter.
OX   NCBI_TaxID=33074 {ECO:0000313|EMBL:BBG30791.1, ECO:0000313|Proteomes:UP000267342};
RN   [1] {ECO:0000313|EMBL:BBG30791.1, ECO:0000313|Proteomes:UP000267342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAM14233 {ECO:0000313|EMBL:BBG30791.1,
RC   ECO:0000313|Proteomes:UP000267342};
RA   Yanase H.;
RT   "Zymobacter palmae IAM14233 (=T109) whole genome analysis.";
RL   Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
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; AP018933; BBG30791.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A348HGN9; -.
DR   STRING; 1123510.GCA_000620025_01205; -.
DR   KEGG; zpl:ZBT109_2045; -.
DR   Proteomes; UP000267342; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
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}; DNA-directed RNA polymerase {ECO:0000313|EMBL:BBG30791.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000267342};
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          140..153
FT                   /note="RNA polymerase sigma-70"
FT                   /evidence="ECO:0000259|PROSITE:PS00715"
FT   DOMAIN          309..335
FT                   /note="RNA polymerase sigma-70"
FT                   /evidence="ECO:0000259|PROSITE:PS00716"
FT   DNA_BIND        310..329
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00959"
FT   REGION          1..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          78..111
FT                   /note="Sigma-70 factor domain-1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00959"
FT   REGION          116..186
FT                   /note="Sigma-70 factor domain-2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00959"
FT   REGION          196..271
FT                   /note="Sigma-70 factor domain-3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00959"
FT   REGION          284..337
FT                   /note="Sigma-70 factor domain-4"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00959"
FT   MOTIF           140..143
FT                   /note="Interaction with polymerase core subunit RpoC"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00959"
FT   COMPBIAS        11..29
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..57
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   351 AA;  40149 MW;  6935AB165087CB8B CRC64;
     MKGNMTMNVV EREVTHKKRP VSPRTTEEDD NLDMVEELEA DDSEDIDAAD AVADDESENE
     AFEKALHREE RQSTSSLDPT QIYLNEIGFS PLLSPEEEVF YGRLARKGDP AGRQRMIESN
     LRLVVKISRR YLNRGLSLLD LIEEGNLGLI RAVEKFDPER GFRFSTYATW WIRQTIERAL
     MNQTRTIRLP IHVVKELNVY LRAARELTQK LDHEATPEDI ATYLDRPVAS VKRMLGLNER
     ISSVDYPVGS DSDKPLIDTI ADDGIAGPES DLVHHDMKAH VDAWLSELSD KQKEVVMRRF
     GLRGYESATL EEVGDEIGLT RERVRQIQVE ALKKLRRMLE GRGLSLDTIF E
//
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