RIMJ_SHIFL
ID RIMJ_SHIFL Reviewed; 194 AA.
AC P0A950; P09454;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 108.
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=SF1072, S1150;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN42694.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP16581.1; -; Genomic_DNA.
DR RefSeq; NP_706987.1; NC_004337.2.
DR RefSeq; WP_000468186.1; NZ_WPGW01000001.1.
DR AlphaFoldDB; P0A950; -.
DR SMR; P0A950; -.
DR STRING; 198214.SF1072; -.
DR EnsemblBacteria; AAN42694; AAN42694; SF1072.
DR EnsemblBacteria; AAP16581; AAP16581; S1150.
DR GeneID; 1024014; -.
DR GeneID; 66670667; -.
DR KEGG; sfl:SF1072; -.
DR KEGG; sfx:S1150; -.
DR PATRIC; fig|198214.7.peg.1255; -.
DR HOGENOM; CLU_013985_40_1_6; -.
DR OMA; AACIPDN; -.
DR OrthoDB; 1501005at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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_0000074569"
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