RNK_ECOLI
ID RNK_ECOLI Reviewed; 136 AA.
AC P0AFW4; P40679;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Regulator of nucleoside diphosphate kinase {ECO:0000255|HAMAP-Rule:MF_00954};
GN Name=rnk {ECO:0000255|HAMAP-Rule:MF_00954};
GN OrderedLocusNames=b0610, JW0602;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND GENE NAME.
RX PubMed=7565093; DOI=10.1111/j.1365-2958.1995.tb02303.x;
RA Schlictman D., Shankar S., Chakrabarty A.M.;
RT "The Escherichia coli genes sspA and rnk can functionally replace the
RT Pseudomonas aeruginosa alginate regulatory gene algR2.";
RL Mol. Microbiol. 16:309-320(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12;
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;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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 [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=8596442; DOI=10.1111/j.1365-2958.1995.mmi_17050935.x;
RA Shankar S., Schlictman D., Chakrabarty A.M.;
RT "Regulation of nucleoside diphosphate kinase and an alternative kinase in
RT Escherichia coli: role of the sspA and rnk genes in nucleoside triphosphate
RT formation.";
RL Mol. Microbiol. 17:935-943(1995).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS), FUNCTION, INTERACTION WITH RNA
RP POLYMERASE, AND DOMAIN.
RX PubMed=18760284; DOI=10.1016/j.jmb.2008.08.011;
RA Lamour V., Rutherford S.T., Kuznedelov K., Ramagopal U.A., Gourse R.L.,
RA Severinov K., Darst S.A.;
RT "Crystal structure of Escherichia coli Rnk, a new RNA polymerase-
RT interacting protein.";
RL J. Mol. Biol. 383:367-379(2008).
CC -!- FUNCTION: May act as an anti-Gre factor. Regulates the level of the
CC nucleoside diphosphate kinase Ndk. {ECO:0000255|HAMAP-Rule:MF_00954,
CC ECO:0000269|PubMed:18760284, ECO:0000269|PubMed:8596442}.
CC -!- SUBUNIT: Interacts with the RNA polymerase. {ECO:0000255|HAMAP-
CC Rule:MF_00954, ECO:0000269|PubMed:18760284}.
CC -!- INTERACTION:
CC P0AFW4; P0ACJ0: lrp; NbExp=4; IntAct=EBI-553769, EBI-1113316;
CC P0AFW4; P77174: ybdM; NbExp=5; IntAct=EBI-553769, EBI-1118992;
CC -!- DOMAIN: Contains a short N-terminal coiled-coil domain and a C-terminal
CC globular domain. {ECO:0000269|PubMed:18760284}.
CC -!- DISRUPTION PHENOTYPE: Mutant shows a significant reduction in the level
CC of Ndk. {ECO:0000269|PubMed:8596442}.
CC -!- MISCELLANEOUS: Can restore alginate synthesis and Ndk activity in the
CC aglQ mutant of P.aeruginosa. {ECO:0000305|PubMed:7565093}.
CC -!- SIMILARITY: Belongs to the Rnk family. {ECO:0000255|HAMAP-
CC Rule:MF_00954}.
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DR EMBL; L37900; AAC36933.1; -; Genomic_DNA.
DR EMBL; U82598; AAB40810.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73711.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35239.1; -; Genomic_DNA.
DR PIR; I57917; I57917.
DR RefSeq; NP_415143.1; NC_000913.3.
DR RefSeq; WP_000089731.1; NZ_STEB01000031.1.
DR PDB; 3BMB; X-ray; 1.91 A; A/B=1-136.
DR PDBsum; 3BMB; -.
DR AlphaFoldDB; P0AFW4; -.
DR SMR; P0AFW4; -.
DR BioGRID; 4259900; 11.
DR BioGRID; 851863; 7.
DR DIP; DIP-48048N; -.
DR IntAct; P0AFW4; 28.
DR STRING; 511145.b0610; -.
DR jPOST; P0AFW4; -.
DR PaxDb; P0AFW4; -.
DR PRIDE; P0AFW4; -.
DR EnsemblBacteria; AAC73711; AAC73711; b0610.
DR EnsemblBacteria; BAA35239; BAA35239; BAA35239.
DR GeneID; 66671115; -.
DR GeneID; 947546; -.
DR KEGG; ecj:JW0602; -.
DR KEGG; eco:b0610; -.
DR PATRIC; fig|1411691.4.peg.1658; -.
DR EchoBASE; EB2518; -.
DR eggNOG; COG0782; Bacteria.
DR HOGENOM; CLU_120358_1_1_6; -.
DR InParanoid; P0AFW4; -.
DR OMA; VHCREES; -.
DR PhylomeDB; P0AFW4; -.
DR BioCyc; EcoCyc:G6337-MON; -.
DR EvolutionaryTrace; P0AFW4; -.
DR PRO; PR:P0AFW4; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0070063; F:RNA polymerase binding; IEA:InterPro.
DR GO; GO:0006354; P:DNA-templated transcription, elongation; IBA:GO_Central.
DR GO; GO:0032784; P:regulation of DNA-templated transcription, elongation; IEA:InterPro.
DR Gene3D; 3.10.50.30; -; 1.
DR HAMAP; MF_00954; Rnk; 1.
DR InterPro; IPR036953; GreA/GreB_C_sf.
DR InterPro; IPR028625; Rnk.
DR InterPro; IPR029462; Rnk_N.
DR InterPro; IPR001437; Tscrpt_elong_fac_GreA/B_C.
DR InterPro; IPR023459; Tscrpt_elong_fac_GreA/B_fam.
DR PANTHER; PTHR30437; PTHR30437; 1.
DR Pfam; PF01272; GreA_GreB; 1.
DR Pfam; PF14760; Rnk_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome.
FT CHAIN 1..136
FT /note="Regulator of nucleoside diphosphate kinase"
FT /id="PRO_0000097386"
FT STRAND 7..9
FT /evidence="ECO:0007829|PDB:3BMB"
FT HELIX 10..21
FT /evidence="ECO:0007829|PDB:3BMB"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:3BMB"
FT HELIX 29..39
FT /evidence="ECO:0007829|PDB:3BMB"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:3BMB"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:3BMB"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:3BMB"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:3BMB"
FT STRAND 70..76
FT /evidence="ECO:0007829|PDB:3BMB"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:3BMB"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:3BMB"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:3BMB"
FT HELIX 93..98
FT /evidence="ECO:0007829|PDB:3BMB"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:3BMB"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:3BMB"
FT STRAND 115..126
FT /evidence="ECO:0007829|PDB:3BMB"
FT TURN 128..132
FT /evidence="ECO:0007829|PDB:3BMB"
SQ SEQUENCE 136 AA; 14927 MW; 7043926623BA5E1E CRC64;
MSRPTIIIND LDAERIDILL EQPAYAGLPI ADALNAELDR AQMCSPEEMP HDVVTMNSRV
KFRNLSDGEV RVRTLVYPAK MTDSNTQLSV MAPVGAALLG LRVGDSIHWE LPGGVATHLE
VLELEYQPEA AGDYLL
