KDPE_ECOLI
ID KDPE_ECOLI Reviewed; 225 AA.
AC P21866; P75739; P76822;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 3.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=KDP operon transcriptional regulatory protein KdpE;
GN Name=kdpE; OrderedLocusNames=b0694, JW5096;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=K12;
RX PubMed=1532388; DOI=10.1128/jb.174.7.2152-2159.1992;
RA Walderhaug M.O., Polarek J.W., Voelkner P., Daniel J.M., Hesse J.E.,
RA Altendorf K., Epstein W.;
RT "KdpD and KdpE, proteins that control expression of the kdpABC operon, are
RT members of the two-component sensor-effector class of regulators.";
RL J. Bacteriol. 174:2152-2159(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
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 [4]
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).
RN [5]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
CC -!- FUNCTION: Member of the two-component regulatory system KdpD/KdpE
CC involved in the regulation of the kdp operon.
CC {ECO:0000269|PubMed:1532388}.
CC -!- INTERACTION:
CC P21866; P21865: kdpD; NbExp=5; IntAct=EBI-6403634, EBI-1123100;
CC P21866; P52108: rstA; NbExp=2; IntAct=EBI-6403634, EBI-558990;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1532388}.
CC -!- PTM: Phosphorylated by KdpD. {ECO:0000305}.
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DR EMBL; M36066; AAA24042.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73788.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35351.2; -; Genomic_DNA.
DR PIR; E64804; E64804.
DR RefSeq; NP_415222.1; NC_000913.3.
DR RefSeq; WP_000186076.1; NZ_SSZK01000045.1.
DR PDB; 1ZH2; X-ray; 2.00 A; A/B=1-121.
DR PDB; 1ZH4; X-ray; 2.20 A; A/B=1-121.
DR PDB; 3ZQ7; X-ray; 2.52 A; A=124-225.
DR PDB; 4KFC; X-ray; 2.53 A; A/B=3-225.
DR PDB; 4KNY; X-ray; 2.94 A; A/B=3-225.
DR PDB; 4L85; X-ray; 2.20 A; A/B/C=3-121.
DR PDB; 6LGQ; X-ray; 3.00 A; D=1-225.
DR PDBsum; 1ZH2; -.
DR PDBsum; 1ZH4; -.
DR PDBsum; 3ZQ7; -.
DR PDBsum; 4KFC; -.
DR PDBsum; 4KNY; -.
DR PDBsum; 4L85; -.
DR PDBsum; 6LGQ; -.
DR AlphaFoldDB; P21866; -.
DR SMR; P21866; -.
DR BioGRID; 4259924; 3.
DR BioGRID; 849679; 1.
DR DIP; DIP-10063N; -.
DR IntAct; P21866; 2.
DR STRING; 511145.b0694; -.
DR jPOST; P21866; -.
DR PaxDb; P21866; -.
DR PRIDE; P21866; -.
DR EnsemblBacteria; AAC73788; AAC73788; b0694.
DR EnsemblBacteria; BAA35351; BAA35351; BAA35351.
DR GeneID; 945302; -.
DR KEGG; ecj:JW5096; -.
DR KEGG; eco:b0694; -.
DR PATRIC; fig|1411691.4.peg.1581; -.
DR EchoBASE; EB0512; -.
DR eggNOG; COG0745; Bacteria.
DR HOGENOM; CLU_000445_30_8_6; -.
DR InParanoid; P21866; -.
DR OMA; MSHPGQL; -.
DR PhylomeDB; P21866; -.
DR BioCyc; EcoCyc:KDPE-MON; -.
DR EvolutionaryTrace; P21866; -.
DR PRO; PR:P21866; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0032993; C:protein-DNA complex; IBA:GO_Central.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:EcoCyc.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; IDA:EcoCyc.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:EcoCyc.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:EcoCyc.
DR CDD; cd00383; trans_reg_C; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR001867; OmpR/PhoB-type_DNA-bd.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR039420; WalR-like.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR48111; PTHR48111; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF00486; Trans_reg_C; 1.
DR SMART; SM00448; REC; 1.
DR SMART; SM00862; Trans_reg_C; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR PROSITE; PS51755; OMPR_PHOB; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA-binding; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Two-component regulatory system.
FT CHAIN 1..225
FT /note="KDP operon transcriptional regulatory protein KdpE"
FT /id="PRO_0000081113"
FT DOMAIN 3..116
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DNA_BIND 126..225
FT /note="OmpR/PhoB-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01091"
FT MOD_RES 52
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT CONFLICT 160..176
FT /note="LAVLLNNAGKVLTQRQL -> AGRCSTMPEKYSPSGPV (in Ref. 1;
FT AAA24042)"
FT /evidence="ECO:0000305"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:1ZH2"
FT HELIX 11..22
FT /evidence="ECO:0007829|PDB:1ZH2"
FT TURN 23..25
FT /evidence="ECO:0007829|PDB:1ZH2"
FT STRAND 27..33
FT /evidence="ECO:0007829|PDB:1ZH2"
FT HELIX 34..44
FT /evidence="ECO:0007829|PDB:1ZH2"
FT STRAND 47..55
FT /evidence="ECO:0007829|PDB:1ZH2"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:4KNY"
FT HELIX 60..68
FT /evidence="ECO:0007829|PDB:1ZH2"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:1ZH2"
FT HELIX 84..93
FT /evidence="ECO:0007829|PDB:1ZH2"
FT STRAND 96..102
FT /evidence="ECO:0007829|PDB:1ZH2"
FT HELIX 105..119
FT /evidence="ECO:0007829|PDB:1ZH2"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:3ZQ7"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:3ZQ7"
FT TURN 138..141
FT /evidence="ECO:0007829|PDB:3ZQ7"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:3ZQ7"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:3ZQ7"
FT HELIX 154..165
FT /evidence="ECO:0007829|PDB:3ZQ7"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:3ZQ7"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:3ZQ7"
FT HELIX 173..180
FT /evidence="ECO:0007829|PDB:3ZQ7"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:3ZQ7"
FT HELIX 189..203
FT /evidence="ECO:0007829|PDB:3ZQ7"
FT STRAND 211..216
FT /evidence="ECO:0007829|PDB:3ZQ7"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:3ZQ7"
FT STRAND 220..223
FT /evidence="ECO:0007829|PDB:3ZQ7"
SQ SEQUENCE 225 AA; 25362 MW; 6C2D029F82706F6D CRC64;
MTNVLIVEDE QAIRRFLRTA LEGDGMRVFE AETLQRGLLE AATRKPDLII LDLGLPDGDG
IEFIRDLRQW SAVPVIVLSA RSEESDKIAA LDAGADDYLS KPFGIGELQA RLRVALRRHS
ATTAPDPLVK FSDVTVDLAA RVIHRGEEEV HLTPIEFRLL AVLLNNAGKV LTQRQLLNQV
WGPNAVEHSH YLRIYMGHLR QKLEQDPARP RHFITETGIG YRFML
