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Database: UniProt
Entry: A0A6I4SSF6_9SPHN
LinkDB: A0A6I4SSF6_9SPHN
Original site: A0A6I4SSF6_9SPHN 
ID   A0A6I4SSF6_9SPHN        Unreviewed;       687 AA.
AC   A0A6I4SSF6;
DT   12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT   12-AUG-2020, sequence version 1.
DT   18-JUN-2025, entry version 17.
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:MXO58795.1};
GN   ORFNames=GRI89_04475 {ECO:0000313|EMBL:MXO58795.1};
OS   Croceibacterium salegens.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Sphingomonadales; Erythrobacteraceae; Croceibacterium.
OX   NCBI_TaxID=1737568 {ECO:0000313|EMBL:MXO58795.1, ECO:0000313|Proteomes:UP000433652};
RN   [1] {ECO:0000313|EMBL:MXO58795.1, ECO:0000313|Proteomes:UP000433652}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCCC 1K01500 {ECO:0000313|EMBL:MXO58795.1,
RC   ECO:0000313|Proteomes:UP000433652};
RA   Xu L.;
RT   "Genomic-based taxomic classification of the family Erythrobacteraceae.";
RL   Submitted (DEC-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}.
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:MXO58795.1}.
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DR   EMBL; WTYM01000030; MXO58795.1; -; Genomic_DNA.
DR   RefSeq; WP_159792603.1; NZ_WTYM01000030.1.
DR   AlphaFoldDB; A0A6I4SSF6; -.
DR   OrthoDB; 9809557at2; -.
DR   Proteomes; UP000433652; 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   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   FunFam; 1.10.601.10:FF:000001; 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   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:UP000433652};
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          477..490
FT                   /note="RNA polymerase sigma-70"
FT                   /evidence="ECO:0000259|PROSITE:PS00715"
FT   DOMAIN          646..672
FT                   /note="RNA polymerase sigma-70"
FT                   /evidence="ECO:0000259|PROSITE:PS00716"
FT   DNA_BIND        647..666
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          49..130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          201..267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          453..523
FT                   /note="Sigma-70 factor domain-2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   REGION          532..608
FT                   /note="Sigma-70 factor domain-3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   REGION          621..674
FT                   /note="Sigma-70 factor domain-4"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   MOTIF           477..480
FT                   /note="Interaction with polymerase core subunit RpoC"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   COMPBIAS        52..62
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        77..106
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        115..130
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..221
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        232..251
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   687 AA;  78038 MW;  38ADE93CC8903292 CRC64;
     MASDDTTKGN GSDSGNDDAP LIDLNEASIK KLISKAKRKG YITVDELNAA LPEDELSSEQ
     IEDVMSAISE MGVNVVESDE DAQEEDDESG DGPDEINSAD DDDDDDGPKA NQNVPEKKKA
     ATTERTDDPV RMYLREMGAV ELLSREGEIA IAKRIEAGRD TMIMGLCESP ITFHAIIMWS
     EALNNEEMQL REILDLDAML SKEPPVDKME EGAEDDDDGE ISEATAGPTI REDDEVEDHE
     EENDEDDEDG EGGSSRRREE DDEEDNTMSL AQMEAALKPD ALERFDRITK LFKKFEKIQG
     ERVDVLGRGE EFGAAKEKKY EELREELTAE VEAVQFHATK IEYLVDNLYA FNRRLTALGG
     QMLRLAERHK VKRLDFLNEY VGNELDEAWL AAMAKKDKKW AAFAEKEADT VERIRAEIAD
     IASQTGMSLN EFRRIVNMVQ KGEREARIAK KEMVEANLRL VISIAKKYTN RGLQFLDLIQ
     EGNIGLMKAV DKFEYRRGYK FSTYATWWIR QAITRSIADQ ARTIRIPVHM IETINKLVRT
     SRQFLHEQGR EPTPEEMAER LSMPLEKVRK VMKIAKEPIS LETPIGDEED SHLGDFIEDK
     NAVIPVDAAI QANLKETVTR VLASLTPREE RVLRMRFGIG MNTDHTLEEV GQQFSVTRER
     IRQIEAKALR KLKHPSRSRK MRSFLDQ
//
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