PAT_MYCS2
ID PAT_MYCS2 Reviewed; 333 AA.
AC A0R3F9;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Acetyltransferase Pat;
DE EC=2.3.1.-;
DE AltName: Full=GCN5-related N-acetyltransferase;
DE Short=GNAT;
DE AltName: Full=Protein acetyltransferase;
DE Short=Pat;
GN OrderedLocusNames=MSMEG_5458, MSMEI_5308;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP FUNCTION, MUTAGENESIS OF ARG-95 AND GLU-234, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, DISRUPTION PHENOTYPE, AND
RP SUBUNIT.
RX PubMed=20507997; DOI=10.1074/jbc.m110.118398;
RA Nambi S., Basu N., Visweswariah S.S.;
RT "cAMP-regulated protein lysine acetylases in mycobacteria.";
RL J. Biol. Chem. 285:24313-24323(2010).
RN [5]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RX PubMed=21627103; DOI=10.1021/bi200156t;
RA Xu H., Hegde S.S., Blanchard J.S.;
RT "Reversible acetylation and inactivation of Mycobacterium tuberculosis
RT acetyl-CoA synthetase is dependent on cAMP.";
RL Biochemistry 50:5883-5892(2011).
CC -!- FUNCTION: Catalyzes specifically the acetylation of the epsilon-amino
CC group of a highly conserved lysine residue in acetyl-CoA synthetase
CC (ACS) and of the universal stress protein (USP) MSMEG_4207. Acetylation
CC results in the inactivation of ACS activity and could be important for
CC mycobacteria to adjust to environmental changes.
CC {ECO:0000269|PubMed:20507997, ECO:0000269|PubMed:21627103}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- ACTIVITY REGULATION: Allosterically regulated by cAMP.
CC {ECO:0000269|PubMed:20507997, ECO:0000269|PubMed:21627103}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.1 uM for acetyl-CoA (with ACS as substrate)
CC {ECO:0000269|PubMed:20507997, ECO:0000269|PubMed:21627103};
CC KM=10 uM for acetyl-CoA (with USP as substrate)
CC {ECO:0000269|PubMed:20507997, ECO:0000269|PubMed:21627103};
CC KM=10.2 uM for ACS {ECO:0000269|PubMed:20507997,
CC ECO:0000269|PubMed:21627103};
CC KM=335 uM for USP {ECO:0000269|PubMed:20507997,
CC ECO:0000269|PubMed:21627103};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20507997}.
CC -!- DISRUPTION PHENOTYPE: Disruption of this gene abolishes acetylation of
CC USP. {ECO:0000269|PubMed:20507997}.
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DR EMBL; CP000480; ABK70370.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP41750.1; -; Genomic_DNA.
DR RefSeq; WP_003896854.1; NZ_SIJM01000006.1.
DR RefSeq; YP_889697.1; NC_008596.1.
DR PDB; 4OLL; X-ray; 1.90 A; A=2-333.
DR PDB; 4ONU; X-ray; 2.25 A; A=2-333.
DR PDB; 4ORF; X-ray; 2.00 A; A=2-333.
DR PDBsum; 4OLL; -.
DR PDBsum; 4ONU; -.
DR PDBsum; 4ORF; -.
DR AlphaFoldDB; A0R3F9; -.
DR SMR; A0R3F9; -.
DR STRING; 246196.MSMEI_5308; -.
DR EnsemblBacteria; ABK70370; ABK70370; MSMEG_5458.
DR EnsemblBacteria; AFP41750; AFP41750; MSMEI_5308.
DR GeneID; 66736761; -.
DR KEGG; msg:MSMEI_5308; -.
DR KEGG; msm:MSMEG_5458; -.
DR PATRIC; fig|246196.19.peg.5319; -.
DR eggNOG; COG0664; Bacteria.
DR eggNOG; COG1670; Bacteria.
DR OMA; MVHIPGI; -.
DR OrthoDB; 655439at2; -.
DR BRENDA; 2.3.1.B34; 3512.
DR SABIO-RK; A0R3F9; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008080; F:N-acetyltransferase activity; IDA:CACAO.
DR CDD; cd00038; CAP_ED; 1.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR018488; cNMP-bd_CS.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR Pfam; PF13302; Acetyltransf_3; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR SMART; SM00100; cNMP; 1.
DR SUPFAM; SSF51206; SSF51206; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS00889; CNMP_BINDING_2; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Magnesium; Metal-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..333
FT /note="Acetyltransferase Pat"
FT /id="PRO_0000420361"
FT DOMAIN 153..317
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT BINDING 85..88
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:O05581"
FT BINDING 95..96
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:O05581"
FT BINDING 135
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:O05581"
FT BINDING 211
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O05581"
FT BINDING 237..239
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O05581"
FT BINDING 245..250
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O05581"
FT BINDING 276
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O05581"
FT BINDING 285
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O05581"
FT MUTAGEN 95
FT /note="R->K: No increase in the rate of acetylation in the
FT presence of cAMP, presumably because of its inability to
FT bind cAMP."
FT /evidence="ECO:0000269|PubMed:20507997"
FT MUTAGEN 234
FT /note="E->A: Shows a lower rate of acetylation of USP in
FT the absence of cAMP than the wild-type protein, but in the
FT presence of cAMP, an increase in the rate of
FT acetyltransferase activity is observed."
FT /evidence="ECO:0000269|PubMed:20507997"
FT HELIX 4..13
FT /evidence="ECO:0007829|PDB:4OLL"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:4OLL"
FT HELIX 23..26
FT /evidence="ECO:0007829|PDB:4OLL"
FT HELIX 27..30
FT /evidence="ECO:0007829|PDB:4OLL"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:4OLL"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:4OLL"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:4OLL"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:4OLL"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:4OLL"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:4ORF"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:4OLL"
FT HELIX 86..91
FT /evidence="ECO:0007829|PDB:4OLL"
FT STRAND 97..103
FT /evidence="ECO:0007829|PDB:4OLL"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:4OLL"
FT HELIX 112..120
FT /evidence="ECO:0007829|PDB:4OLL"
FT HELIX 124..137
FT /evidence="ECO:0007829|PDB:4OLL"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:4OLL"
FT STRAND 152..157
FT /evidence="ECO:0007829|PDB:4OLL"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:4OLL"
FT TURN 181..184
FT /evidence="ECO:0007829|PDB:4OLL"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:4OLL"
FT HELIX 190..198
FT /evidence="ECO:0007829|PDB:4OLL"
FT STRAND 202..212
FT /evidence="ECO:0007829|PDB:4OLL"
FT STRAND 217..227
FT /evidence="ECO:0007829|PDB:4OLL"
FT STRAND 231..239
FT /evidence="ECO:0007829|PDB:4OLL"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:4OLL"
FT TURN 244..247
FT /evidence="ECO:0007829|PDB:4OLL"
FT HELIX 248..263
FT /evidence="ECO:0007829|PDB:4OLL"
FT STRAND 267..272
FT /evidence="ECO:0007829|PDB:4OLL"
FT HELIX 277..284
FT /evidence="ECO:0007829|PDB:4OLL"
FT TURN 285..287
FT /evidence="ECO:0007829|PDB:4OLL"
FT STRAND 298..303
FT /evidence="ECO:0007829|PDB:4OLL"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:4OLL"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:4OLL"
FT HELIX 314..330
FT /evidence="ECO:0007829|PDB:4OLL"
SQ SEQUENCE 333 AA; 36848 MW; C6CCBC36F639C945 CRC64;
MAELTEVRAA DLAALEFFTG CRPSALEPLA TQLRPLKAEP GQVLIRQGDP ALTFMLIESG
RVQVSHAVAD GPPIVLDIEP GLIIGEIALL RDAPRTATVV AAEPVIGWVG DRDAFDTILH
LPGMFDRLVR IARQRLAAFI TPIPVQVRTG EWFYLRPVLP GDVERTLNGP VEFSSETLYR
RFQSVRKPTR ALLEYLFEVD YADHFVWVMT EGALGPVIAD ARFVREGHNA TMAEVAFTVG
DDYQGRGIGS FLMGALIVSA NYVGVQRFNA RVLTDNMAMR KIMDRLGAVW VREDLGVVMT
EVDVPPVDTV PFEPELIDQI RDATRKVIRA VSQ
