ID A0A0N1EPL9_9GAMM Unreviewed; 498 AA.
AC A0A0N1EPL9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=RNA polymerase sigma-54 factor {ECO:0000256|ARBA:ARBA00019942, ECO:0000256|PIRNR:PIRNR000774};
GN ORFNames=ADS77_02235 {ECO:0000313|EMBL:KPH65113.1};
OS Pseudoalteromonas porphyrae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=187330 {ECO:0000313|EMBL:KPH65113.1, ECO:0000313|Proteomes:UP000037848};
RN [1] {ECO:0000313|EMBL:KPH65113.1, ECO:0000313|Proteomes:UP000037848}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCD-SED14 {ECO:0000313|EMBL:KPH65113.1,
RC ECO:0000313|Proteomes:UP000037848};
RA Coil D.A., Jospin G., Lee R.D., Eisen J.A.;
RT "Draft Genome Sequence of Pseudoalteromonas porphyrae UCD-SED14.";
RL Submitted (AUG-2015) 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. {ECO:0000256|PIRNR:PIRNR000774}.
CC -!- SIMILARITY: Belongs to the sigma-54 factor family.
CC {ECO:0000256|ARBA:ARBA00008798, ECO:0000256|PIRNR:PIRNR000774}.
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:KPH65113.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LHPH01000002; KPH65113.1; -; Genomic_DNA.
DR RefSeq; WP_054204412.1; NZ_LITL01000007.1.
DR AlphaFoldDB; A0A0N1EPL9; -.
DR STRING; 187330.AMS58_07445; -.
DR PATRIC; fig|187330.3.peg.477; -.
DR OrthoDB; 9814402at2; -.
DR Proteomes; UP000037848; Unassembled WGS sequence.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; IEA:InterPro.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016987; F:sigma factor activity; IEA:UniProtKB-KW.
DR GO; GO:0006352; P:DNA-templated transcription initiation; IEA:InterPro.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 1.10.10.1330; RNA polymerase sigma-54 factor, core-binding domain; 1.
DR InterPro; IPR000394; RNA_pol_sigma_54.
DR InterPro; IPR007046; RNA_pol_sigma_54_core-bd.
DR InterPro; IPR007634; RNA_pol_sigma_54_DNA-bd.
DR InterPro; IPR038709; RpoN_core-bd_sf.
DR NCBIfam; TIGR02395; rpoN_sigma; 1.
DR PANTHER; PTHR32248; RNA POLYMERASE SIGMA-54 FACTOR; 1.
DR PANTHER; PTHR32248:SF4; RNA POLYMERASE SIGMA-54 FACTOR; 1.
DR Pfam; PF00309; Sigma54_AID; 1.
DR Pfam; PF04963; Sigma54_CBD; 1.
DR Pfam; PF04552; Sigma54_DBD; 1.
DR PIRSF; PIRSF000774; RpoN; 1.
DR PRINTS; PR00045; SIGMA54FCT.
DR PROSITE; PS00717; SIGMA54_1; 1.
DR PROSITE; PS00718; SIGMA54_2; 1.
DR PROSITE; PS50044; SIGMA54_3; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PIRNR:PIRNR000774};
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|PIRNR:PIRNR000774};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|PIRNR:PIRNR000774};
KW Sigma factor {ECO:0000256|ARBA:ARBA00023082,
KW ECO:0000256|PIRNR:PIRNR000774};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|PIRNR:PIRNR000774};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|PIRNR:PIRNR000774};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000774}.
FT DOMAIN 132..324
FT /note="RNA polymerase sigma factor 54 core-binding"
FT /evidence="ECO:0000259|Pfam:PF04963"
FT DOMAIN 338..495
FT /note="RNA polymerase sigma factor 54 DNA-binding"
FT /evidence="ECO:0000259|Pfam:PF04552"
FT REGION 42..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..68
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 498 AA; 55884 MW; 09FB1842AEC89261 CRC64;
MRQSLQLRMG QQLTMTPQLQ QAIRLLQLST LDLQQEIQEA LDSNPLLEVD ENDFGDESGG
KNEQKQDTDD QTVSASADDT PSEYEQESSE ALAKDTVSDE MAMDVTWDEY MSAAPSSSSG
PMPEDESIYQ GASSETLHDH LMWQLQLTHF SPTDEAIAIA IVEAVDDSGI LTLSCEDIAE
SLNKGNNEEE IELDEVQAVL KRIQLFDPVG IAARSLPECL CIQLNQFDPA TPWIAETKMI
LTDHIDLLAS RDYRTLMKKT KLKEDELKEV MTLIHSLNPK PADTIVREES EYVIPDVSVK
KIKGRWVVEL NPDSMPKIRV NSQYAAMSRS VKSSTDSQFI RSHLQEAKWF IKSLESRNDT
LLKVTNCIVK QQQGFFEHGP EAMRPMVLND VAEMVEMHES TISRVTTQKY MHTPRGIFEL
KYFFSSHVST ENGGECSSTA IRALIKKLIA AENSAKPLSD SKIADILAEQ GIKVARRTIA
KYRESLAIPP SNQRKSLI
//