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Database: UniProt
Entry: A0A1B3PRB9_9BURK
LinkDB: A0A1B3PRB9_9BURK
Original site: A0A1B3PRB9_9BURK 
ID   A0A1B3PRB9_9BURK        Unreviewed;       536 AA.
AC   A0A1B3PRB9;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=RNA polymerase sigma-54 factor {ECO:0000256|PIRNR:PIRNR000774};
GN   Name=rpoN {ECO:0000313|EMBL:AOG25324.1};
GN   ORFNames=BSY15_1115 {ECO:0000313|EMBL:AOG25324.1};
OS   Acidovorax sp. RAC01.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=1842533 {ECO:0000313|EMBL:AOG25324.1, ECO:0000313|Proteomes:UP000094760};
RN   [1] {ECO:0000313|Proteomes:UP000094760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RAC01 {ECO:0000313|Proteomes:UP000094760};
RA   Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL   Submitted (JUL-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; CP016447; AOG25324.1; -; Genomic_DNA.
DR   RefSeq; WP_069103953.1; NZ_CP016447.1.
DR   AlphaFoldDB; A0A1B3PRB9; -.
DR   STRING; 1842533.BSY15_1115; -.
DR   KEGG; acra:BSY15_1115; -.
DR   PATRIC; fig|1842533.3.peg.1158; -.
DR   OrthoDB; 9814402at2; -.
DR   Proteomes; UP000094760; Chromosome.
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   Reference proteome {ECO:0000313|Proteomes:UP000094760};
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          145..363
FT                   /note="RNA polymerase sigma factor 54 core-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04963"
FT   DOMAIN          379..534
FT                   /note="RNA polymerase sigma factor 54 DNA-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04552"
FT   REGION          44..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        44..60
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        79..101
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        128..144
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   536 AA;  58772 MW;  668DD3C2137FCE3D CRC64;
     MKPGLSLRVS QHLALTPQLQ QSIRLLQLST LELSQEVEQM LDENPFLERT AEEAPREEFG
     LDAADAPPQA DDYSADDAIF SGASSTTATS PEGQNESETP SGAGDEPDWS GDGTVEMAPN
     DAEWGGDAPP RTRNDSEGDE ADATELARSH ESLTAFLHRQ ALGLRLSEVD CAALRFLIES
     LNDDGYLEES LEELAITLAG PDDLEQIEEL VHRFTVAQRL LQSLEPVGVG ARGLAECLTL
     QLQAMAADED GPADAATVQT ALRICQQPLE MLAKRDVRRL TVLCSEGGAS GEERTRAAMA
     LIARLEPRPG RRFADVERNI IIPDVIVRKA GREGAQRGRD TQQNFIVQLN PDVMPRLRVH
     DIYAGALRGH KGGEGHQGMQ QRLQEARWFI KNIQQRFDTI LRVSRAIVER QKSFFTHGEL
     AMRPLVLRDI ADELGLHEST ISRVTTAKYM ATPIGTYELK YFFGSGLGTE TGGNASSTAV
     RALIKQFVAA ENAAKPLSDS QIAEMLKEQG IECARRTVAK YREALKIAPA NLRKTL
//
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