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Database: UniProt
Entry: V5YUG8_SERMA
LinkDB: V5YUG8_SERMA
Original site: V5YUG8_SERMA 
ID   V5YUG8_SERMA            Unreviewed;       635 AA.
AC   V5YUG8;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 55.
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:BAO21012.1};
GN   ORFNames=BVG97_18920 {ECO:0000313|EMBL:ASL89541.1};
OS   Serratia marcescens.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=615 {ECO:0000313|EMBL:BAO21012.1};
RN   [1] {ECO:0000313|EMBL:BAO21012.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IOMTU 115 {ECO:0000313|EMBL:BAO21012.1};
RA   Tada T., Miyoshi-Akiyama T., Kirikae T.;
RT   "Genetic environments surrounding aac(6')-Ial.";
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ASL89541.1, ECO:0000313|Proteomes:UP000198428}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UMH5 {ECO:0000313|EMBL:ASL89541.1,
RC   ECO:0000313|Proteomes:UP000198428};
RX   PubMed=28536292;
RA   Anderson M.T., Mitchell L.A., Zhao L., Mobley H.L.T.;
RT   "Capsule Production and Glucose Metabolism Dictate Fitness during Serratia
RT   marcescens Bacteremia.";
RL   MBio 8:e00740-e00717(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 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; CP018917; ASL89541.1; -; Genomic_DNA.
DR   EMBL; AB894481; BAO21012.1; -; Genomic_DNA.
DR   AlphaFoldDB; V5YUG8; -.
DR   Proteomes; UP000198428; 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   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; IPR028630; Sigma70_RpoD.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   NCBIfam; TIGR02393; RpoD_Cterm; 1.
DR   NCBIfam; TIGR02937; sigma70-ECF; 1.
DR   PANTHER; PTHR30603; RNA POLYMERASE SIGMA FACTOR RPO; 1.
DR   PANTHER; PTHR30603:SF47; RNA POLYMERASE SIGMA FACTOR SIGF, CHLOROPLASTIC; 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};
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          425..438
FT                   /note="RNA polymerase sigma-70"
FT                   /evidence="ECO:0000259|PROSITE:PS00715"
FT   DOMAIN          594..620
FT                   /note="RNA polymerase sigma-70"
FT                   /evidence="ECO:0000259|PROSITE:PS00716"
FT   DNA_BIND        595..614
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   REGION          202..238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          401..471
FT                   /note="Sigma-70 factor domain-2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   REGION          480..556
FT                   /note="Sigma-70 factor domain-3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   REGION          569..622
FT                   /note="Sigma-70 factor domain-4"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   MOTIF           425..428
FT                   /note="Interaction with polymerase core subunit RpoC"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   COMPBIAS        211..233
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   635 AA;  72640 MW;  8B32CFD50C536B4E CRC64;
     MLLLAVSPTD TNLNTLKCGY RLMEQNPQSQ LKLLVTRGKE QGYLTYAEVN DHLPEDIVDS
     DQIEDIIQMI NDMGIQVMEE APDADDLLLA ENSNSTDEDA EEAAAQVLSS VESEIGRTTD
     PVRMYMREMG TVELLTREGE IDIAKRIEDG INQVQCSVAE YPEAITYLLE QYDRVEAGEA
     RLSDLITGFV DPNAEEDIAP TATHIGSELS SEEQDDDEED EDDEDDDTED DNSIDPELAR
     QKFAELRDQY EATRLVIKKN GRSHASAADE ILKLSEVFKQ FRLVPKQFDF LVNSMRTMMD
     RVRTQERIIM KLCVEQCKMP KKNFVTLFAG NETSDSWFEA ALAMAKPWSE KLKDVAEDVQ
     RSLQKLRQIE EETGLTIEQV KDINRRMSIG EAKARRAKKE MVEANLRLVI SIAKKYTNRG
     LQFLDLIQEG NIGLMKAVDK FEYRRGYKFS TYATWWIRQA ITRSIADQAR TIRIPVHMIE
     TINKLNRISR QMLQEMGREP TPEELAERML MPEDKIRKVL KIAKEPISME TPIGDDEDSH
     LGDFIEDTTL ELPLDSATSE SLRSATHDVL AGLTAREAKV LRMRFGIDMN TDHTLEEVGK
     QFDVTRERIR QIEAKALRKL RHPSRSEVLR SFLDD
//
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