RIMJ_ECOLI
ID RIMJ_ECOLI Reviewed; 194 AA.
AC P0A948; P09454;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=[Ribosomal protein S5]-alanine N-acetyltransferase {ECO:0000305};
DE EC=2.3.1.267 {ECO:0000269|PubMed:2828880};
DE AltName: Full=Acetylating enzyme for N-terminal of ribosomal protein S5;
GN Name=rimJ {ECO:0000303|PubMed:385889}; OrderedLocusNames=b1066, JW1053;
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 CATALYTIC ACTIVITY.
RC STRAIN=K12;
RX PubMed=2828880; DOI=10.1007/bf00331153;
RA Yoshikawa A., Isono S., Sheback A., Isono K.;
RT "Cloning and nucleotide sequencing of the genes rimI and rimJ which encode
RT enzymes acetylating ribosomal proteins S18 and S5 of Escherichia coli
RT K12.";
RL Mol. Gen. Genet. 209:481-488(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=K12;
RX PubMed=1356970; DOI=10.1128/jb.174.21.7003-7012.1992;
RA White-Ziegler C.A., Low D.A.;
RT "Thermoregulation of the pap operon: evidence for the involvement of RimJ,
RT the N-terminal acetylase of ribosomal protein S5.";
RL J. Bacteriol. 174:7003-7012(1992).
RN [3]
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 [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=385889; DOI=10.1016/0022-2836(79)90072-x;
RA Cumberlidge A.G., Isono K.;
RT "Ribosomal protein modification in Escherichia coli. I. A mutant lacking
RT the N-terminal acetylation of protein S5 exhibits thermosensitivity.";
RL J. Mol. Biol. 131:169-189(1979).
RN [7]
RP FUNCTION IN RIBOSOME BIOGENESIS, OVEREXPRESSION, INTERACTION WITH PRE-30S
RP SUBUNITS, AND MUTAGENESIS OF CYS-54 AND CYS-105.
RX PubMed=18466225; DOI=10.1111/j.1365-2958.2008.06252.x;
RA Roy-Chaudhuri B., Kirthi N., Kelley T., Culver G.M.;
RT "Suppression of a cold-sensitive mutation in ribosomal protein S5 reveals a
RT role for RimJ in ribosome biogenesis.";
RL Mol. Microbiol. 68:1547-1559(2008).
RN [8]
RP FUNCTION IN RIBOSOME BIOGENESIS, AND OVEREXPRESSION.
RX PubMed=20176963; DOI=10.1073/pnas.0912305107;
RA Roy-Chaudhuri B., Kirthi N., Culver G.M.;
RT "Appropriate maturation and folding of 16S rRNA during 30S subunit
RT biogenesis are critical for translational fidelity.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:4567-4572(2010).
CC -!- FUNCTION: Acetylates the N-terminal alanine of ribosomal protein S5
CC (PubMed:385889, PubMed:2828880). Also plays a role in maturation of the
CC 30S ribosomal subunit (PubMed:18466225, PubMed:20176963). Plays a role
CC in the temperature regulation of pap pilin transcription
CC (PubMed:1356970). {ECO:0000269|PubMed:1356970,
CC ECO:0000269|PubMed:18466225, ECO:0000269|PubMed:20176963,
CC ECO:0000269|PubMed:2828880, ECO:0000269|PubMed:385889}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-alanyl-[ribosomal protein uS5] = CoA
CC + H(+) + N-terminal N(alpha)-acetyl-L-alanyl-[ribosomal protein uS5];
CC Xref=Rhea:RHEA:43752, Rhea:RHEA-COMP:10672, Rhea:RHEA-COMP:10673,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:64718, ChEBI:CHEBI:83683; EC=2.3.1.267;
CC Evidence={ECO:0000269|PubMed:2828880};
CC -!- SUBUNIT: Associates with pre-30S subunits.
CC {ECO:0000269|PubMed:18466225}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Mutation of the gene impairs the acetylation of
CC the N-terminal alanine of ribosomal protein S5 (PubMed:385889). Mutant
CC is thermosensitive (PubMed:385889). {ECO:0000269|PubMed:385889}.
CC -!- MISCELLANEOUS: Overexpression suppresses the cold-sensitive phenotype
CC associated with the ribosomal protein S5 G28D mutation.
CC {ECO:0000269|PubMed:18466225, ECO:0000269|PubMed:20176963}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. RimJ subfamily.
CC {ECO:0000305}.
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DR EMBL; X06118; CAA29490.1; -; Genomic_DNA.
DR EMBL; M99278; AAA24549.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74150.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35874.1; -; Genomic_DNA.
DR PIR; S01084; S01084.
DR RefSeq; NP_415584.1; NC_000913.3.
DR RefSeq; WP_000468186.1; NZ_STEB01000016.1.
DR AlphaFoldDB; P0A948; -.
DR SMR; P0A948; -.
DR BioGRID; 4260076; 61.
DR DIP; DIP-35985N; -.
DR IntAct; P0A948; 17.
DR STRING; 511145.b1066; -.
DR jPOST; P0A948; -.
DR PaxDb; P0A948; -.
DR PRIDE; P0A948; -.
DR EnsemblBacteria; AAC74150; AAC74150; b1066.
DR EnsemblBacteria; BAA35874; BAA35874; BAA35874.
DR GeneID; 66670667; -.
DR GeneID; 946910; -.
DR KEGG; ecj:JW1053; -.
DR KEGG; eco:b1066; -.
DR PATRIC; fig|1411691.4.peg.1202; -.
DR EchoBASE; EB0844; -.
DR eggNOG; COG1670; Bacteria.
DR HOGENOM; CLU_013985_40_1_6; -.
DR InParanoid; P0A948; -.
DR OMA; AACIPDN; -.
DR PhylomeDB; P0A948; -.
DR BioCyc; EcoCyc:EG10851-MON; -.
DR BioCyc; MetaCyc:EG10851-MON; -.
DR BRENDA; 2.3.1.267; 2026.
DR PRO; PR:P0A948; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0008080; F:N-acetyltransferase activity; IMP:EcoliWiki.
DR GO; GO:1990189; F:peptide-serine-N-acetyltransferase activity; IDA:EcoCyc.
DR GO; GO:0008999; F:ribosomal protein S5-alanine N-acetyltransferase activity; IMP:EcoliWiki.
DR GO; GO:0017189; P:N-terminal peptidyl-alanine acetylation; IMP:EcoCyc.
DR GO; GO:0017198; P:N-terminal peptidyl-serine acetylation; IDA:EcoCyc.
DR GO; GO:0006474; P:N-terminal protein amino acid acetylation; IMP:EcoliWiki.
DR GO; GO:0042254; P:ribosome biogenesis; IMP:EcoCyc.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR Pfam; PF13302; Acetyltransf_3; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..194
FT /note="[Ribosomal protein S5]-alanine N-acetyltransferase"
FT /id="PRO_0000074567"
FT DOMAIN 18..188
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT MUTAGEN 54
FT /note="C->A: Loss of acetyltransferase activity but can
FT still suppress the S5(G28D) defects; when associated with
FT A-105."
FT /evidence="ECO:0000269|PubMed:18466225"
FT MUTAGEN 54
FT /note="C->F: Loss of acetyltransferase activity."
FT /evidence="ECO:0000269|PubMed:18466225"
FT MUTAGEN 105
FT /note="C->A: Loss of acetyltransferase activity. Can still
FT suppress the S5(G28D) defects; when associated with A-54."
FT /evidence="ECO:0000269|PubMed:18466225"
SQ SEQUENCE 194 AA; 22688 MW; 1DCC58BD1C06AB61 CRC64;
MFGYRSNVPK VRLTTDRLVV RLVHDRDAWR LADYYAENRH FLKPWEPVRD ESHCYPSGWQ
ARLGMINEFH KQGSAFYFGL FDPDEKEIIG VANFSNVVRG SFHACYLGYS IGQKWQGKGL
MFEALTAAIR YMQRTQHIHR IMANYMPHNK RSGDLLARLG FEKEGYAKDY LLIDGQWRDH
VLTALTTPDW TPGR
