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Database: UniProt
Entry: Q9KJ96_PSEYM
LinkDB: Q9KJ96_PSEYM
Original site: Q9KJ96_PSEYM 
ID   Q9KJ96_PSEYM            Unreviewed;       497 AA.
AC   Q9KJ96;
DT   01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2000, sequence version 1.
DT   24-JAN-2024, entry version 73.
DE   RecName: Full=RNA polymerase sigma-54 factor {ECO:0000256|ARBA:ARBA00019942, ECO:0000256|PIRNR:PIRNR000774};
GN   Name=rpoN {ECO:0000313|EMBL:AAF29509.1};
OS   Pseudomonas syringae pv. maculicola.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=59511 {ECO:0000313|EMBL:AAF29509.1};
RN   [1] {ECO:0000313|EMBL:AAF29509.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Psm ES4326 {ECO:0000313|EMBL:AAF29509.1};
RX   PubMed=10852883; DOI=10.1128/JB.182.12.3498-3507.2000;
RA   Hendrickson E.L., Guevera P., Penaloza-Vazquez A., Shao J., Bender C.,
RA   Ausubel F.M.;
RT   "Virulence of the phytopathogen Pseudomonas syringae pv. maculicola is rpoN
RT   dependent.";
RL   J. Bacteriol. 182:3498-3507(2000).
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; AF199600; AAF29509.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9KJ96; -.
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          130..323
FT                   /note="RNA polymerase sigma factor 54 core-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04963"
FT   DOMAIN          337..495
FT                   /note="RNA polymerase sigma factor 54 DNA-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04552"
FT   REGION          43..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   497 AA;  56633 MW;  CBADC06A07B8C98E CRC64;
     MKPSLVLRMG QQLTMTPQLQ QAIRLLQLST LDLQQEIQEA LESNPMLERQ EEGDDFDNSD
     PLADNIEQKP NPDVQEPTYQ EAAPTVDNLE DGEWGERIPN ELPVDTAWED VYQTSASSLP
     SSDDDEWDFT TRTSVGESLQ SHLLWQLNVA PMSDKDRLVA VTLIDCINNQ GYLDETLEEI
     LESFDPELDV ELDEIEAVLH RIQQFEPAGI GARNLSECLL LQLRQLPART PWLAEAQRLV
     TEYIDLLGSR DYAQLMRRMK IKEDELRQVI ELVQSLNPRP GSQIESTEAE YVIPDVIVRK
     DNERWLVELN QESVPRLRVN PQYAGFVRRA DTSADNTFMH NQLQEARWFI KSLQSRFETL
     MKVATQIVEH QRGFLEYGDE AMKPLVLHDI AEAVGMHEST ISRVTTQKFM HTPRGIYELK
     YFFSSHVSTS EGGECSSTAI RAIIKKLVAA ENQKKPLSDS KIAGLLEAQG IQVARRTVAK
     YRESLGIAPS SERKRLM
//
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