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Database: UniProt
Entry: A0A1I5TXU1_9PSED
LinkDB: A0A1I5TXU1_9PSED
Original site: A0A1I5TXU1_9PSED 
ID   A0A1I5TXU1_9PSED        Unreviewed;       502 AA.
AC   A0A1I5TXU1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=RNA polymerase sigma-54 factor {ECO:0000256|ARBA:ARBA00019942, ECO:0000256|PIRNR:PIRNR000774};
GN   ORFNames=SAMN05216190_12249 {ECO:0000313|EMBL:SFP87870.1};
OS   Pseudomonas borbori.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=289003 {ECO:0000313|EMBL:SFP87870.1, ECO:0000313|Proteomes:UP000198784};
RN   [1] {ECO:0000313|Proteomes:UP000198784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17834 {ECO:0000313|Proteomes:UP000198784};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FOWX01000022; SFP87870.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I5TXU1; -.
DR   STRING; 289003.SAMN05216190_12249; -.
DR   OrthoDB; 9814402at2; -.
DR   Proteomes; UP000198784; 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          134..328
FT                   /note="RNA polymerase sigma factor 54 core-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04963"
FT   DOMAIN          342..500
FT                   /note="RNA polymerase sigma factor 54 DNA-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04552"
FT   REGION          43..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        71..94
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   502 AA;  57104 MW;  8B92D37CA3A49645 CRC64;
     MKPSLVLKMG QQLTMTPQLQ QAIRLLQLST LDLQQEIQEA LESNPMLERE EDGDDFDNSN
     PLADGAENPT PAPQQEESYQ DNSHQETPQT VDNLEEGEWN ERIPNELPVD TAWEDVYQTS
     ASSLPSNDDD EWDFTTRTST GESLQSHLLW QLNLVPMSDK DRLIGVTLID CINYQGYLEE
     SLEEVVAAFD PELDIELDEV EAVLHRIQQF EPAGIAARDL RECLLLQLRQ LPAKTPWLAE
     AQRLANDYLD LLGSRDYSQL MRRMKIKEDE LRQVIELIQS LNPRPGSQIE SSEPEYVVPD
     VIVRKHNERW LVELNQEAMP RLRVNAQYAG FVKRADSSAD NTFMRNQLQE ARWFIKSLQS
     RNETLMKVAS QIVEHQRGFL DYGDEAMKPL VLHDIAEAVG MHESTISRVT TQKFMHTPRG
     IYELKYFFSS HVSTAEGGEC SSTAIRAIIK KLVAAENAKK PLSDSKIAGL LEAQGIQVAR
     RTVAKYRESL GIAPSSERKR LM
//
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