PTAS_STAAR
ID PTAS_STAAR Reviewed; 328 AA.
AC Q6GJ80;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Phosphate acetyltransferase;
DE EC=2.3.1.8;
DE AltName: Full=Phosphotransacetylase;
GN Name=pta; OrderedLocusNames=SAR0594;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + phosphate = acetyl phosphate + CoA;
CC Xref=Rhea:RHEA:19521, ChEBI:CHEBI:22191, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.8;
CC -!- PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis;
CC acetyl-CoA from acetate: step 2/2.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the phosphate acetyltransferase and
CC butyryltransferase family. {ECO:0000305}.
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DR EMBL; BX571856; CAG39614.1; -; Genomic_DNA.
DR RefSeq; WP_000774291.1; NC_002952.2.
DR PDB; 4E4R; X-ray; 1.44 A; A=1-328.
DR PDBsum; 4E4R; -.
DR AlphaFoldDB; Q6GJ80; -.
DR SMR; Q6GJ80; -.
DR KEGG; sar:SAR0594; -.
DR HOGENOM; CLU_019723_0_1_9; -.
DR OMA; TMLVKMG; -.
DR OrthoDB; 1301815at2; -.
DR BRENDA; 2.3.1.8; 3352.
DR UniPathway; UPA00340; UER00459.
DR Proteomes; UP000000596; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008959; F:phosphate acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006085; P:acetyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.10750; -; 1.
DR Gene3D; 3.40.50.10950; -; 1.
DR InterPro; IPR012147; P_Ac_Bu_trans.
DR InterPro; IPR004614; P_AcTrfase.
DR InterPro; IPR042113; P_AcTrfase_dom1.
DR InterPro; IPR042112; P_AcTrfase_dom2.
DR InterPro; IPR002505; PTA_PTB.
DR Pfam; PF01515; PTA_PTB; 1.
DR PIRSF; PIRSF000428; P_Ac_trans; 1.
DR TIGRFAMs; TIGR00651; pta; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Cytoplasm; Transferase.
FT CHAIN 1..328
FT /note="Phosphate acetyltransferase"
FT /id="PRO_0000179143"
FT HELIX 1..12
FT /evidence="ECO:0007829|PDB:4E4R"
FT STRAND 17..21
FT /evidence="ECO:0007829|PDB:4E4R"
FT HELIX 27..37
FT /evidence="ECO:0007829|PDB:4E4R"
FT STRAND 39..48
FT /evidence="ECO:0007829|PDB:4E4R"
FT HELIX 50..59
FT /evidence="ECO:0007829|PDB:4E4R"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:4E4R"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:4E4R"
FT HELIX 78..88
FT /evidence="ECO:0007829|PDB:4E4R"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:4E4R"
FT HELIX 95..101
FT /evidence="ECO:0007829|PDB:4E4R"
FT HELIX 105..114
FT /evidence="ECO:0007829|PDB:4E4R"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:4E4R"
FT HELIX 133..139
FT /evidence="ECO:0007829|PDB:4E4R"
FT STRAND 150..157
FT /evidence="ECO:0007829|PDB:4E4R"
FT STRAND 160..169
FT /evidence="ECO:0007829|PDB:4E4R"
FT HELIX 175..191
FT /evidence="ECO:0007829|PDB:4E4R"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:4E4R"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:4E4R"
FT HELIX 212..230
FT /evidence="ECO:0007829|PDB:4E4R"
FT STRAND 236..241
FT /evidence="ECO:0007829|PDB:4E4R"
FT HELIX 243..247
FT /evidence="ECO:0007829|PDB:4E4R"
FT HELIX 249..255
FT /evidence="ECO:0007829|PDB:4E4R"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:4E4R"
FT HELIX 273..285
FT /evidence="ECO:0007829|PDB:4E4R"
FT STRAND 290..297
FT /evidence="ECO:0007829|PDB:4E4R"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:4E4R"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:4E4R"
FT HELIX 312..326
FT /evidence="ECO:0007829|PDB:4E4R"
SQ SEQUENCE 328 AA; 35015 MW; 2F875831DD08C097 CRC64;
MADLLNVLKD KLSGKNVKIV LPEGEDERVL TAATQLQATD YVTPIVLGDE TKVQSLAQKL
NLDISNIELI NPATSELKAE LVQSFVERRK GKTTEEQAQE LLNNVNYFGT MLVYAGKADG
LVSGAAHSTG DTVRPALQII KTKPGVSRTS GIFFMIKGDE QYIFGDCAIN PELDSQGLAE
IAVESAKSAL SFGMDPKVAM LSFSTKGSAK SDDVTKVQEA VKLAQQKAEE EKLEAIIDGE
FQFDAAIVPG VAEKKAPGAK LQGDANVFVF PSLEAGNIGY KIAQRLGGYD AVGPVLQGLN
SPVNDLSRGC SIEDVYNLSF ITAAQALQ
