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Database: UniProt
Entry: A0A5B7YG34_9ALTE
LinkDB: A0A5B7YG34_9ALTE
Original site: A0A5B7YG34_9ALTE 
ID   A0A5B7YG34_9ALTE        Unreviewed;       612 AA.
AC   A0A5B7YG34;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2019, sequence version 1.
DT   18-JUN-2025, entry version 23.
DE   RecName: Full=RNA polymerase sigma factor RpoD {ECO:0000256|HAMAP-Rule:MF_00963};
DE   AltName: Full=Sigma-70 {ECO:0000256|HAMAP-Rule:MF_00963};
GN   Name=rpoD {ECO:0000256|HAMAP-Rule:MF_00963,
GN   ECO:0000313|EMBL:QCZ94564.1};
GN   ORFNames=FBQ74_14295 {ECO:0000313|EMBL:QCZ94564.1};
OS   Salinimonas iocasae.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Alteromonadales; Alteromonadaceae; Alteromonas/Salinimonas group;
OC   Salinimonas.
OX   NCBI_TaxID=2572577 {ECO:0000313|EMBL:QCZ94564.1, ECO:0000313|Proteomes:UP000304912};
RN   [1] {ECO:0000313|EMBL:QCZ94564.1, ECO:0000313|Proteomes:UP000304912}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KX18D6 {ECO:0000313|EMBL:QCZ94564.1,
RC   ECO:0000313|Proteomes:UP000304912};
RA   Zhang H., Wang H., Li C.;
RT   "Salinimonas iocasae sp. nov., a halophilic bacterium isolated from the
RT   outer tube casing of tubeworms in Okinawa Trough.";
RL   Submitted (APR-2019) 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 primary sigma factor during
CC       exponential growth. {ECO:0000256|HAMAP-Rule:MF_00963}.
CC   -!- SUBUNIT: Interacts transiently with the RNA polymerase catalytic core.
CC       {ECO:0000256|HAMAP-Rule:MF_00963}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00963}.
CC   -!- SIMILARITY: Belongs to the sigma-70 factor family. RpoD/SigA subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00963}.
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DR   EMBL; CP039852; QCZ94564.1; -; Genomic_DNA.
DR   RefSeq; WP_139757301.1; NZ_CP039852.1.
DR   AlphaFoldDB; A0A5B7YG34; -.
DR   KEGG; salk:FBQ74_14295; -.
DR   OrthoDB; 9809557at2; -.
DR   Proteomes; UP000304912; 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   FunFam; 1.10.220.120:FF:000001; RNA polymerase sigma factor RpoD; 1.
DR   FunFam; 1.10.601.10:FF:000002; RNA polymerase sigma factor RpoD; 1.
DR   FunFam; 1.10.10.10:FF:000002; RNA polymerase sigma factor SigA; 1.
DR   FunFam; 1.10.10.10:FF:000004; RNA polymerase sigma factor SigA; 1.
DR   Gene3D; 1.10.601.10; RNA Polymerase Primary Sigma Factor; 1.
DR   Gene3D; 1.10.220.120; Sigma-70 factor, region 1.1; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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; IPR007631; RNA_pol_sigma_70_non-ess.
DR   InterPro; IPR007127; RNA_pol_sigma_70_r1_1.
DR   InterPro; IPR042189; RNA_pol_sigma_70_r1_1_sf.
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; IPR050239; Sigma-70_RNA_pol_init_factors.
DR   InterPro; IPR028630; Sigma70_RpoD.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   NCBIfam; NF004208; PRK05658.1; 1.
DR   NCBIfam; TIGR02393; RpoD_Cterm; 1.
DR   NCBIfam; TIGR02937; sigma70-ECF; 1.
DR   PANTHER; PTHR30603; RNA POLYMERASE SIGMA FACTOR RPO; 1.
DR   PANTHER; PTHR30603:SF60; RNA POLYMERASE SIGMA FACTOR RPOD; 1.
DR   Pfam; PF04546; Sigma70_ner; 1.
DR   Pfam; PF03979; Sigma70_r1_1; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00963};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00963}; Reference proteome {ECO:0000313|Proteomes:UP000304912};
KW   Sigma factor {ECO:0000256|ARBA:ARBA00023082, ECO:0000256|HAMAP-
KW   Rule:MF_00963};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW   Rule:MF_00963};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015, ECO:0000256|HAMAP-
KW   Rule:MF_00963}.
FT   DOMAIN          402..415
FT                   /note="RNA polymerase sigma-70"
FT                   /evidence="ECO:0000259|PROSITE:PS00715"
FT   DOMAIN          571..597
FT                   /note="RNA polymerase sigma-70"
FT                   /evidence="ECO:0000259|PROSITE:PS00716"
FT   DNA_BIND        572..591
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   REGION          169..217
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          378..448
FT                   /note="Sigma-70 factor domain-2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   REGION          457..533
FT                   /note="Sigma-70 factor domain-3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   REGION          546..599
FT                   /note="Sigma-70 factor domain-4"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   COILED          329..377
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOTIF           402..405
FT                   /note="Interaction with polymerase core subunit RpoC"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   COMPBIAS        185..211
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   612 AA;  69759 MW;  CDF59D8928D288C7 CRC64;
     MAQSKQSQIK LLIAKGKEQG YLTFAEVNDH LPQDIVDSDQ IEDIIRMIND MGIQVSESAP
     DSDELLMQET TADEDAAEAA AQALATVESE IGRTTDPVRM YMREMGTVEL LTREGEIEIA
     KRIEDGINQV QCSVAEYPEA ITYLLEQWDL YEAEEIRLGD IISGFVDPDD DRDLAPTATH
     IGSELSEEEL EDEDDDDKDD DDDSDEDDSG VDPEQAREKF AELRDQYGKA RDVIETQGRA
     HPDSRKEIAA LSEIFKEFRL VPKQFDRMVK NMRDMMDKVR IQERLVMKYS VINAKMPKKD
     FIKAFAGNET STEWLGEAIN GSHAYSDALA QHKEDIERSV SKMTQVEQET GLIIADIKDI
     NRRMSIGEAK ARRAKKEMVE ANLRLVISIA KKYTNRGLQF LDLIQEGNIG LMKAVDKFEY
     RRGYKFSTYA TWWIRQAITR SIADQARTIR IPVHMIETIN KLNRISRQML QEMGREPSPE
     ELSERMLMPE DKIRKVLKIA KEPISMETPI GDDEDSHLGD FIEDSTIIQP LDSATGGSLK
     GATQEVLAGL TAREAKVLRM RFGIDMNTDH TLEEVGKQFD VTRERIRQIE AKALRKLRHP
     SRSEQLRSFL DE
//
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