YCHF_ECOLI
ID YCHF_ECOLI Reviewed; 363 AA.
AC P0ABU2; P31216; P76018;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Ribosome-binding ATPase YchF {ECO:0000255|HAMAP-Rule:MF_00944};
GN Name=ychF {ECO:0000255|HAMAP-Rule:MF_00944}; Synonyms=engD, gtp1;
GN OrderedLocusNames=b1203, JW1194;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
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 [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-269.
RC STRAIN=K12;
RX PubMed=7828865; DOI=10.1016/0378-1119(94)90647-5;
RA Galindo J.M., de la Vega F.M., Guarneros G.;
RT "Open reading frames flanking the peptidyl-tRNA hydrolase-encoding gene of
RT Escherichia coli.";
RL Gene 151:153-156(1994).
RN [5]
RP PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-173.
RC STRAIN=K12;
RX PubMed=1833189; DOI=10.1002/j.1460-2075.1991.tb04919.x;
RA Garcia-Villegas M.R., de la Vega F.M., Galindo J.M., Segura M.,
RA Buckingham R.H., Guarneros G.;
RT "Peptidyl-tRNA hydrolase is involved in lambda inhibition of host protein
RT synthesis.";
RL EMBO J. 10:3549-3555(1991).
RN [6]
RP PROTEIN SEQUENCE OF 2-13.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [7]
RP IDENTIFICATION.
RA Koonin E., Rudd K.E.;
RL Unpublished observations (APR-1993).
RN [8]
RP FUNCTION, ATPASE ACTIVITY, ACTIVITY REGULATION, SUBUNIT, AND MUTAGENESIS OF
RP ASN-12 AND LYS-78.
RC STRAIN=K12;
RX PubMed=21527254; DOI=10.1016/j.bbrc.2011.04.052;
RA Tomar S.K., Kumar P., Prakash B.;
RT "Deciphering the catalytic machinery in a universally conserved ribosome
RT binding ATPase YchF.";
RL Biochem. Biophys. Res. Commun. 408:459-464(2011).
CC -!- FUNCTION: ATPase that binds to both the 70S ribosome and the 50S
CC ribosomal subunit in a nucleotide-independent manner. Does not
CC hydrolyze GTP. {ECO:0000255|HAMAP-Rule:MF_00944,
CC ECO:0000269|PubMed:21527254}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: ATPase activity is stimulated by potassium and
CC other monovalent cations. Stimulation is maximal in the presence of
CC K(+), followed by NH(4)(+), Rb(+), Na(+) and Cs(+).
CC {ECO:0000269|PubMed:21527254}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:21527254}.
CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase
CC superfamily. OBG GTPase family. YchF/OLA1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00944}.
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DR EMBL; U00096; AAC74287.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA36061.1; -; Genomic_DNA.
DR EMBL; X61941; CAA43946.1; -; Genomic_DNA.
DR EMBL; U02423; AAA67557.1; -; Genomic_DNA.
DR PIR; H64866; H64866.
DR RefSeq; NP_415721.1; NC_000913.3.
DR RefSeq; WP_000505866.1; NZ_STEB01000023.1.
DR AlphaFoldDB; P0ABU2; -.
DR SMR; P0ABU2; -.
DR BioGRID; 4260106; 36.
DR IntAct; P0ABU2; 6.
DR STRING; 511145.b1203; -.
DR SWISS-2DPAGE; P0ABU2; -.
DR jPOST; P0ABU2; -.
DR PaxDb; P0ABU2; -.
DR PRIDE; P0ABU2; -.
DR EnsemblBacteria; AAC74287; AAC74287; b1203.
DR EnsemblBacteria; BAA36061; BAA36061; BAA36061.
DR GeneID; 66674977; -.
DR GeneID; 945769; -.
DR KEGG; ecj:JW1194; -.
DR KEGG; eco:b1203; -.
DR PATRIC; fig|1411691.4.peg.1081; -.
DR EchoBASE; EB1376; -.
DR eggNOG; COG0012; Bacteria.
DR HOGENOM; CLU_018395_0_1_6; -.
DR InParanoid; P0ABU2; -.
DR OMA; VLRCFDN; -.
DR PhylomeDB; P0ABU2; -.
DR BioCyc; EcoCyc:EG11404-MON; -.
DR BioCyc; MetaCyc:EG11404-MON; -.
DR PRO; PR:P0ABU2; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:EcoCyc.
DR GO; GO:0004857; F:enzyme inhibitor activity; IMP:EcoCyc.
DR GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043023; F:ribosomal large subunit binding; IDA:EcoCyc.
DR GO; GO:0043022; F:ribosome binding; IDA:EcoCyc.
DR GO; GO:0006979; P:response to oxidative stress; IMP:EcoCyc.
DR CDD; cd04867; TGS_YchF_OLA1; 1.
DR CDD; cd01900; YchF; 1.
DR Gene3D; 1.10.150.300; -; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00944; YchF_OLA1_ATPase; 1.
DR InterPro; IPR004396; ATPase_YchF/OLA1.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR031167; G_OBG.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004095; TGS.
DR InterPro; IPR012676; TGS-like.
DR InterPro; IPR023192; TGS-like_dom_sf.
DR InterPro; IPR013029; YchF_C.
DR InterPro; IPR041706; YchF_N.
DR Pfam; PF01926; MMR_HSR1; 1.
DR Pfam; PF06071; YchF-GTPase_C; 1.
DR PIRSF; PIRSF006641; CHP00092; 1.
DR PRINTS; PR00326; GTP1OBG.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF81271; SSF81271; 1.
DR TIGRFAMs; TIGR00092; TIGR00092; 1.
DR PROSITE; PS51710; G_OBG; 1.
DR PROSITE; PS51880; TGS; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Direct protein sequencing; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298646"
FT CHAIN 2..363
FT /note="Ribosome-binding ATPase YchF"
FT /id="PRO_0000201675"
FT DOMAIN 3..256
FT /note="OBG-type G"
FT DOMAIN 278..361
FT /note="TGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT BINDING 12..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00944"
FT BINDING 16
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 36
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MUTAGEN 12
FT /note="N->A: Shows similar hydrolysis activities in the
FT presence of K(+) or Na(+)."
FT /evidence="ECO:0000269|PubMed:21527254"
FT MUTAGEN 78
FT /note="K->A: Shows similar hydrolysis activities in the
FT presence of K(+) or Na(+)."
FT /evidence="ECO:0000269|PubMed:21527254"
FT MUTAGEN 78
FT /note="K->R: Retains K(+)-dependent stimulation of ATPase
FT activity and differentiates between K(+) and Na(+)."
FT /evidence="ECO:0000269|PubMed:21527254"
SQ SEQUENCE 363 AA; 39667 MW; 9C2DAFFAC7586F53 CRC64;
MGFKCGIVGL PNVGKSTLFN ALTKAGIEAA NFPFCTIEPN TGVVPMPDPR LDQLAEIVKP
QRTLPTTMEF VDIAGLVKGA SKGEGLGNQF LTNIRETEAI GHVVRCFEND NIIHVSGKVN
PADDIEVINT ELALADLDTC ERAIHRVQKK AKGGDKDAKA ELAVLEKCLP QLENAGMLRA
LDLSAEEKAA IRYLSFLTLK PTMYIANVNE DGFENNPYLD QVREIAAKEG SVVVPVCAAV
EADIAELDDE ERDEFMQELG LEEPGLNRVI RAGYKLLNLQ TYFTAGVKEV RAWTIPVGAT
APQAAGKIHT DFEKGFIRAQ TISFEDFITY KGEQGAKEAG KMRAEGKDYI VKDGDVMNFL
FNV
