YIHI_ECOLI
ID YIHI_ECOLI Reviewed; 169 AA.
AC P0A8H6; P32130; Q2M8G3;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Der GTPase-activating protein YihI;
DE Short=GAP;
GN Name=yihI; OrderedLocusNames=b3866, JW3837;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Wachi M., Hamano-Takaku F., Nagano K., Kobayashi M., Yukawa H., Nagai K.;
RL Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8346018; DOI=10.1093/nar/21.15.3391;
RA Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome. III. DNA sequence of the region
RT from 87.2 to 89.2 minutes.";
RL Nucleic Acids Res. 21:3391-3398(1993).
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 FUNCTION IN LARGE RIBOSOMAL SUBUNIT ASSEMBLY, SUBUNIT, INTERACTION WITH
RP DER/ENGA, INDUCTION, MUTAGENESIS OF ARG-65; ARG-135; ARG-164 AND ARG-167,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=20434458; DOI=10.1016/j.jmb.2010.04.040;
RA Hwang J., Inouye M.;
RT "A bacterial GAP-like protein, YihI, regulating the GTPase of Der, an
RT essential GTP-binding protein in Escherichia coli.";
RL J. Mol. Biol. 399:759-772(2010).
CC -!- FUNCTION: A GTPase-activating protein (GAP) that modifies Der/EngA
CC GTPase function, negatively regulating cell growth, probably via
CC ribosome assembly. Stimulates the GTPase activity of Der; a construct
CC missing the first 45 residues is even more stimulatory. Does not
CC stimulate 2 other GTPases (ObgE and Era). Overexpression inhibits cell
CC growth; precursor 16S rRNA accumulates, the 23S rRNA is 6-7 bases
CC longer than usual, and 50S ribosomal subunits are improperly assembled,
CC leading to 45S subunits lacking proteins L9, L18 and L25.
CC Overexpression of Der in the same cells suppresses the 50S subunit
CC assembly defect, corroborating that YihI and Der interact.
CC {ECO:0000269|PubMed:20434458}.
CC -!- SUBUNIT: Homodimer. Interacts with Der/EngA via the last 78 residues.
CC Interaction with Der occurs at a 1:1 stoichiometry, suggesting the
CC dimer dissociates to interact with Der. {ECO:0000269|PubMed:20434458}.
CC -!- INTERACTION:
CC P0A8H6; P0A8A8: rimP; NbExp=2; IntAct=EBI-552497, EBI-561065;
CC P0A8H6; P37634: rlmJ; NbExp=2; IntAct=EBI-552497, EBI-548165;
CC -!- INDUCTION: Highly expressed during the lag phase, not expressed in
CC later phases. {ECO:0000269|PubMed:20434458}.
CC -!- DISRUPTION PHENOTYPE: Dispensable for cell growth, cells lacking this
CC gene have a shorter lag phase. {ECO:0000269|PubMed:20434458}.
CC -!- MISCELLANEOUS: This is a highly hydrophilic protein; there is a stretch
CC of highly charged residues in the N-terminus and a stretch of acidic
CC residues in the C-terminus.
CC -!- SIMILARITY: Belongs to the YihI family. {ECO:0000305}.
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DR EMBL; D16509; BAA03960.1; -; Genomic_DNA.
DR EMBL; L19201; AAB03000.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76863.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77443.1; -; Genomic_DNA.
DR PIR; S40811; S40811.
DR RefSeq; NP_418302.1; NC_000913.3.
DR RefSeq; WP_001295266.1; NZ_SSZK01000026.1.
DR AlphaFoldDB; P0A8H6; -.
DR SMR; P0A8H6; -.
DR BioGRID; 4262990; 17.
DR BioGRID; 852660; 1.
DR DIP; DIP-47963N; -.
DR IntAct; P0A8H6; 28.
DR STRING; 511145.b3866; -.
DR jPOST; P0A8H6; -.
DR PaxDb; P0A8H6; -.
DR PRIDE; P0A8H6; -.
DR EnsemblBacteria; AAC76863; AAC76863; b3866.
DR EnsemblBacteria; BAE77443; BAE77443; BAE77443.
DR GeneID; 66672229; -.
DR GeneID; 948363; -.
DR KEGG; ecj:JW3837; -.
DR KEGG; eco:b3866; -.
DR PATRIC; fig|1411691.4.peg.2847; -.
DR EchoBASE; EB1781; -.
DR eggNOG; COG3078; Bacteria.
DR HOGENOM; CLU_094104_2_0_6; -.
DR OMA; ENNECLN; -.
DR PhylomeDB; P0A8H6; -.
DR BioCyc; EcoCyc:EG11835-MON; -.
DR BioCyc; MetaCyc:EG11835-MON; -.
DR PRO; PR:P0A8H6; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005096; F:GTPase activator activity; IDA:EcoCyc.
DR GO; GO:0090071; P:negative regulation of ribosome biogenesis; IMP:EcoCyc.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:EcoCyc.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR HAMAP; MF_01058; GAP_YihI; 1.
DR InterPro; IPR007336; YihI.
DR Pfam; PF04220; YihI; 1.
PE 1: Evidence at protein level;
KW GTPase activation; Reference proteome; Ribosome biogenesis.
FT CHAIN 1..169
FT /note="Der GTPase-activating protein YihI"
FT /id="PRO_0000209582"
FT REGION 1..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1..45
FT /note="Not required for interaction with Der/Enga"
FT REGION 17..45
FT /note="Arg/Lys rich"
FT REGION 144..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..157
FT /note="Asp/Glu rich"
FT COMPBIAS 17..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 65
FT /note="R->A: No change in ability to stimulate Der GTPase."
FT /evidence="ECO:0000269|PubMed:20434458"
FT MUTAGEN 135
FT /note="R->A: No change in ability to stimulate Der GTPase."
FT /evidence="ECO:0000269|PubMed:20434458"
FT MUTAGEN 164
FT /note="R->A: No change in ability to stimulate Der GTPase."
FT /evidence="ECO:0000269|PubMed:20434458"
FT MUTAGEN 167
FT /note="R->A: No change in ability to stimulate Der GTPase."
FT /evidence="ECO:0000269|PubMed:20434458"
SQ SEQUENCE 169 AA; 19059 MW; 31C1DF0C07AD9D07 CRC64;
MKPSSSNSRS KGHAKARRKT REELDQEARD RKRQKKRRGH APGSRAAGGN TTSGSKGQNA
PKDPRIGSKT PIPLGVTEKV TKQHKPKSEK PMLSPQAELE LLETDERLDA LLERLEAGET
LSAEEQSWVD AKLDRIDELM QKLGLSYDDD EEEEEDEKQE DMMRLLRGN
