RIMJ_ECO57
ID RIMJ_ECO57 Reviewed; 194 AA.
AC P0A949; P09454;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=[Ribosomal protein S5]-alanine N-acetyltransferase {ECO:0000250|UniProtKB:P0A948};
DE EC=2.3.1.267 {ECO:0000250|UniProtKB:P0A948};
GN Name=rimJ; OrderedLocusNames=Z1703, ECs1444;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: Acetylates the N-terminal alanine of ribosomal protein S5.
CC {ECO:0000250|UniProtKB:P0A948}.
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:0000250|UniProtKB:P0A948};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0A948}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. RimJ subfamily.
CC {ECO:0000305}.
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DR EMBL; AE005174; AAG55812.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB34867.1; -; Genomic_DNA.
DR PIR; D99809; D99809.
DR PIR; H85668; H85668.
DR RefSeq; NP_309471.1; NC_002695.1.
DR RefSeq; WP_000468186.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0A949; -.
DR SMR; P0A949; -.
DR STRING; 155864.EDL933_1642; -.
DR DNASU; 959405; -.
DR EnsemblBacteria; AAG55812; AAG55812; Z1703.
DR EnsemblBacteria; BAB34867; BAB34867; ECs_1444.
DR GeneID; 66670667; -.
DR GeneID; 912337; -.
DR KEGG; ece:Z1703; -.
DR KEGG; ecs:ECs_1444; -.
DR PATRIC; fig|386585.9.peg.1545; -.
DR eggNOG; COG1670; Bacteria.
DR HOGENOM; CLU_013985_40_1_6; -.
DR OMA; AACIPDN; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008999; F:ribosomal protein S5-alanine N-acetyltransferase activity; IEA:UniProtKB-EC.
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 3: Inferred from homology;
KW Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..194
FT /note="[Ribosomal protein S5]-alanine N-acetyltransferase"
FT /id="PRO_0000074568"
FT DOMAIN 18..188
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
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