ID E0J2P2_ECOLW Unreviewed; 477 AA.
AC E0J2P2;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=RNA polymerase sigma-54 factor {ECO:0000256|ARBA:ARBA00019942, ECO:0000256|PIRNR:PIRNR000774};
GN Name=rpoN {ECO:0000313|EMBL:ADT76835.1};
GN OrderedLocusNames=ECW_m3474 {ECO:0000313|EMBL:ADT76835.1};
OS Escherichia coli (strain ATCC 9637 / CCM 2024 / DSM 1116 / LMG 11080 / NBRC
OS 13500 / NCIMB 8666 / NRRL B-766 / W).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=566546 {ECO:0000313|EMBL:ADT76835.1, ECO:0000313|Proteomes:UP000008525};
RN [1] {ECO:0000313|EMBL:ADT76835.1, ECO:0000313|Proteomes:UP000008525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9637 / CCM 2024 / DSM 1116 / LMG 11080 / NBRC 13500 /
RC NCIMB 8666 / NRRL B-766 / W {ECO:0000313|Proteomes:UP000008525};
RX PubMed=21208457; DOI=10.1186/1471-2164-12-9;
RA Archer C.T., Kim J.F., Jeong H., Park J.H., Vickers C.E., Lee S.Y.,
RA Nielsen L.K.;
RT "The genome sequence of E. coli W (ATCC 9637): comparative genome analysis
RT and an improved genome-scale reconstruction of E. coli.";
RL BMC Genomics 12:9-9(2011).
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; CP002185; ADT76835.1; -; Genomic_DNA.
DR RefSeq; WP_000809051.1; NZ_WBMH01000005.1.
DR AlphaFoldDB; E0J2P2; -.
DR SMR; E0J2P2; -.
DR GeneID; 75206058; -.
DR KEGG; elw:ECW_m3474; -.
DR PATRIC; fig|566546.30.peg.3531; -.
DR Proteomes; UP000008525; 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 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 116..303
FT /note="RNA polymerase sigma factor 54 core-binding"
FT /evidence="ECO:0000259|Pfam:PF04963"
FT DOMAIN 317..475
FT /note="RNA polymerase sigma factor 54 DNA-binding"
FT /evidence="ECO:0000259|Pfam:PF04552"
FT REGION 45..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 477 AA; 53994 MW; 764E47276D028461 CRC64;
MKQGLQLRLS QQLAMTPQLQ QAIRLLQLST LELQQELQQA LESNPLLEQI DTHEEIDTRE
TQDSETLDTA DALEQKEMPE ELPLDASWDT IYTAGTPSGT SGDYIDDELP VYQGETTQTL
QDYLMWQVEL TPFSDTDRAI ATSIVDAVDD TGYLTVPLED ILESMGDEEI DIDEVEAVLK
RIQRFDPVGV AAKDLRDCLL IQLSQFDKTT PWLEEARLII SDHLDLLANH DFRTLMRVTR
LKEDVLKEAV NLIQSLDPRP GQSIQTGEPE YVIPDVLVRK HNGHWTVELN SDSIPRLQIN
QHYASMCNNA RNDGDSQFIR SNLQDAKWLI KSLESRNDTL LRVSRCIVEQ QQAFFEQGEE
YMKPMVLADI AQAVEMHEST ISRVTTQKYL HSPRGIFELK YFFSSHVNTE GGGEASSTAI
RALVKKLIAA ENPAKPLSDS KLTSLLSEQG IMVARRTVAK YRESLSIPPS NQRKQLV
//
