RIMJ_PSEAE
ID RIMJ_PSEAE Reviewed; 189 AA.
AC Q9I2H6;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 109.
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=PA1928;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE004091; AAG05316.1; -; Genomic_DNA.
DR PIR; E83404; E83404.
DR RefSeq; NP_250618.1; NC_002516.2.
DR RefSeq; WP_003119171.1; NZ_QZGE01000033.1.
DR AlphaFoldDB; Q9I2H6; -.
DR SMR; Q9I2H6; -.
DR STRING; 287.DR97_5917; -.
DR PaxDb; Q9I2H6; -.
DR PRIDE; Q9I2H6; -.
DR DNASU; 882063; -.
DR EnsemblBacteria; AAG05316; AAG05316; PA1928.
DR GeneID; 882063; -.
DR KEGG; pae:PA1928; -.
DR PATRIC; fig|208964.12.peg.2009; -.
DR PseudoCAP; PA1928; -.
DR HOGENOM; CLU_013985_40_1_6; -.
DR InParanoid; Q9I2H6; -.
DR OMA; AACIPDN; -.
DR PhylomeDB; Q9I2H6; -.
DR BioCyc; PAER208964:G1FZ6-1968-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0008999; F:ribosomal protein S5-alanine N-acetyltransferase activity; IBA:GO_Central.
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..189
FT /note="[Ribosomal protein S5]-alanine N-acetyltransferase"
FT /id="PRO_0000287810"
FT DOMAIN 31..182
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ SEQUENCE 189 AA; 21365 MW; FB81A65FE95A9787 CRC64;
MPGNRRQVPI LHRDADFLLR ALQPDDFVRT SRYENANREH LAPWEPLRDP GYFSVDNARA
RTLLQVASMD EGEALLLLLL DPDDGEVLGR CSYTNIVRGV FQACHLGFSL AAAAQGRGLM
ARALRVANRY CFEQLGLHRI MASHLPRNAR SERLLESLGF EKEGYARAYL KIAGVWEDHV
LRALVDAPR
