ATSE1_PSEAE
ID ATSE1_PSEAE Reviewed; 171 AA.
AC Q9I1K2;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Acetyltransferase PA2271 {ECO:0000303|PubMed:23184347};
DE EC=2.3.1.-;
DE AltName: Full=GCN5-related N-acetyltransferase {ECO:0000303|PubMed:23184347};
DE Short=GNAT {ECO:0000303|PubMed:23184347};
GN OrderedLocusNames=PA2271;
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).
RN [2]
RP FUNCTION, AND SUBSTRATE SPECIFICITY.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=23184347; DOI=10.1002/pro.2199;
RA Kuhn M.L., Majorek K.A., Minor W., Anderson W.F.;
RT "Broad-substrate screen as a tool to identify substrates for bacterial
RT Gcn5-related N-acetyltransferases with unknown substrate specificity.";
RL Protein Sci. 22:222-230(2013).
CC -!- FUNCTION: Catalyzes the transfer of an acetyl group from acetyl
CC coenzyme A (AcCoA) to an acceptor substrate and releases both CoA and
CC the acetylated product. It can use a variety of substrates including
CC spermidine, spermine and N(8)-acetylspermidine, 7-aminocephalosporanic
CC acid, colistin and thiamine. {ECO:0000269|PubMed:23184347}.
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DR EMBL; AE004091; AAG05659.1; -; Genomic_DNA.
DR PIR; H83360; H83360.
DR RefSeq; NP_250961.1; NC_002516.2.
DR RefSeq; WP_003089295.1; NZ_QZGE01000014.1.
DR AlphaFoldDB; Q9I1K2; -.
DR SMR; Q9I1K2; -.
DR STRING; 287.DR97_6162; -.
DR PaxDb; Q9I1K2; -.
DR PRIDE; Q9I1K2; -.
DR DNASU; 879779; -.
DR EnsemblBacteria; AAG05659; AAG05659; PA2271.
DR GeneID; 879779; -.
DR KEGG; pae:PA2271; -.
DR PATRIC; fig|208964.12.peg.2373; -.
DR PseudoCAP; PA2271; -.
DR HOGENOM; CLU_096760_0_0_6; -.
DR InParanoid; Q9I1K2; -.
DR OMA; PRVCMRR; -.
DR PhylomeDB; Q9I1K2; -.
DR BioCyc; PAER208964:G1FZ6-2310-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IDA:UniProtKB.
DR GO; GO:0008999; F:ribosomal protein S5-alanine N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0017189; P:N-terminal peptidyl-alanine acetylation; IBA:GO_Central.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR Pfam; PF13508; Acetyltransf_7; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 4: Predicted;
KW Acyltransferase; Reference proteome; Transferase.
FT CHAIN 1..171
FT /note="Acetyltransferase PA2271"
FT /id="PRO_0000433347"
FT DOMAIN 3..162
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT BINDING 84..86
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q9I0Q8"
FT BINDING 128..130
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q9I0Q8"
SQ SEQUENCE 171 AA; 19165 MW; 07F93719DAA29D2F CRC64;
MDYRIRTSRD EDAALLPAIE RSAGESFRLL PELAWIADAG VAGVDFHRRL IERGSHWLAE
DADGQPVGFL AAERCADELH IAELSIAQAH QQQGLGRRLL ERAVTYAHAS HCRALTLTTF
CDVPWNAPFY ARLGFQRLTW QEAGERLRAI LGHEQEIGFA ADSRCAMRLV L