RP54_ECOLI
ID RP54_ECOLI Reviewed; 477 AA.
AC P24255; Q2M910;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=RNA polymerase sigma-54 factor;
GN Name=rpoN; Synonyms=glnF, ntrA; OrderedLocusNames=b3202, JW3169;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2203540; DOI=10.1016/0092-8674(90)90269-k;
RA Sasse-Dwight S., Gralla J.D.;
RT "Role of eukaryotic-type functional domains found in the prokaryotic
RT enhancer receptor factor sigma 54.";
RL Cell 62:945-954(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=8444818; DOI=10.1128/jb.175.5.1550-1551.1993;
RA Imaishi H., Gomada M., Inouye S., Nakazawa A.;
RT "Physical map location of the rpoN gene of Escherichia coli.";
RL J. Bacteriol. 175:1550-1551(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=8025669; DOI=10.1099/13500872-140-5-1035;
RA Jones D.H.A., Franklin C.F.H., Thomas C.M.;
RT "Molecular analysis of the operon which encodes the RNA polymerase sigma
RT factor sigma 54 of Escherichia coli.";
RL Microbiology 140:1035-1043(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=7876255; DOI=10.1074/jbc.270.9.4822;
RA Powell B.S., Court D.L., Inada T., Nakamura Y., Michotey V., Cui X.,
RA Reizer A., Saier M.H. Jr., Reizer J.;
RT "Novel proteins of the phosphotransferase system encoded within the rpoN
RT operon of Escherichia coli. Enzyme IIANtr affects growth on organic
RT nitrogen and the conditional lethality of an erats mutant.";
RL J. Biol. Chem. 270:4822-4839(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
CC -!- FUNCTION: Sigma factors are initiation factors that promote the
CC attachment of RNA polymerase to specific initiation sites and are then
CC released. This sigma factor is responsible for the expression of
CC enzymes involved in arginine catabolism. The open complex (sigma-54 and
CC core RNA polymerase) serves as the receptor for the receipt of the
CC melting signal from the remotely bound activator protein GlnG(NtrC).
CC -!- SIMILARITY: Belongs to the sigma-54 factor family. {ECO:0000305}.
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; M57612; AAA62790.1; -; Genomic_DNA.
DR EMBL; D12938; BAA02315.1; -; Genomic_DNA.
DR EMBL; Z27094; CAA81617.1; -; Genomic_DNA.
DR EMBL; U12684; AAB60163.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58004.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76234.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77246.1; -; Genomic_DNA.
DR PIR; I57054; A35695.
DR RefSeq; NP_417669.1; NC_000913.3.
DR RefSeq; WP_000809057.1; NZ_SSZK01000007.1.
DR PDB; 2MT3; NMR; -; A=414-477.
DR PDBsum; 2MT3; -.
DR AlphaFoldDB; P24255; -.
DR BMRB; P24255; -.
DR SMR; P24255; -.
DR BioGRID; 4259282; 32.
DR ComplexPortal; CPX-4884; DNA-directed RNA polymerase holoenzyme complex, Sigma54 variant.
DR DIP; DIP-10776N; -.
DR IntAct; P24255; 14.
DR STRING; 511145.b3202; -.
DR jPOST; P24255; -.
DR PaxDb; P24255; -.
DR PRIDE; P24255; -.
DR EnsemblBacteria; AAC76234; AAC76234; b3202.
DR EnsemblBacteria; BAE77246; BAE77246; BAE77246.
DR GeneID; 947714; -.
DR KEGG; ecj:JW3169; -.
DR KEGG; eco:b3202; -.
DR PATRIC; fig|1411691.4.peg.3529; -.
DR EchoBASE; EB0891; -.
DR eggNOG; COG1508; Bacteria.
DR HOGENOM; CLU_020569_0_1_6; -.
DR InParanoid; P24255; -.
DR OMA; VTTQKFM; -.
DR PhylomeDB; P24255; -.
DR BioCyc; EcoCyc:RPON-MON; -.
DR BioCyc; MetaCyc:RPON-MON; -.
DR PRO; PR:P24255; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR CollecTF; EXPREG_00000990; -.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0032993; C:protein-DNA complex; IMP:CollecTF.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; IMP:CollecTF.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016987; F:sigma factor activity; IEA:UniProtKB-KW.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IMP:CollecTF.
DR GO; GO:0006525; P:arginine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0048870; P:cell motility; IC:ComplexPortal.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro.
DR GO; GO:0042128; P:nitrate assimilation; IC:ComplexPortal.
DR GO; GO:0090605; P:submerged biofilm formation; IC:ComplexPortal.
DR DisProt; DP01169; -.
DR Gene3D; 1.10.10.1330; -; 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 PANTHER; PTHR32248; PTHR32248; 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 TIGRFAMs; TIGR02395; rpoN_sigma; 1.
DR PROSITE; PS00717; SIGMA54_1; 1.
DR PROSITE; PS00718; SIGMA54_2; 1.
DR PROSITE; PS50044; SIGMA54_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Arginine metabolism; DNA-binding;
KW DNA-directed RNA polymerase; Nucleotidyltransferase; Reference proteome;
KW Sigma factor; Transcription; Transcription regulation; Transferase.
FT CHAIN 1..477
FT /note="RNA polymerase sigma-54 factor"
FT /id="PRO_0000205529"
FT DNA_BIND 366..385
FT /note="H-T-H motif"
FT /evidence="ECO:0000250"
FT REGION 45..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 454..462
FT /note="RPON box"
FT COMPBIAS 48..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 99..103
FT /note="GTSGD -> APAVT (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT HELIX 416..419
FT /evidence="ECO:0007829|PDB:2MT3"
FT TURN 420..422
FT /evidence="ECO:0007829|PDB:2MT3"
FT HELIX 423..429
FT /evidence="ECO:0007829|PDB:2MT3"
FT HELIX 441..447
FT /evidence="ECO:0007829|PDB:2MT3"
FT TURN 448..450
FT /evidence="ECO:0007829|PDB:2MT3"
FT HELIX 454..465
FT /evidence="ECO:0007829|PDB:2MT3"
SQ SEQUENCE 477 AA; 53990 MW; 1FAA4273A02B34FD CRC64;
MKQGLQLRLS QQLAMTPQLQ QAIRLLQLST LELQQELQQA LESNPLLEQI DTHEEIDTRE
TQDSETLDTA DALEQKEMPE ELPLDASWDT IYTAGTPSGT SGDYIDDELP VYQGETTQTL
QDYLMWQVEL TPFSDTDRAI ATSIVDAVDE TGYLTVPLED ILESIGDEEI 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
