PTAS_STAAM
ID PTAS_STAAM Reviewed; 328 AA.
AC P65862; Q99W23;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Phosphate acetyltransferase;
DE EC=2.3.1.8;
DE AltName: Full=Phosphotransacetylase;
GN Name=pta; OrderedLocusNames=SAV0588;
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
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; BA000017; BAB56750.1; -; Genomic_DNA.
DR RefSeq; WP_000774281.1; NC_002758.2.
DR AlphaFoldDB; P65862; -.
DR SMR; P65862; -.
DR World-2DPAGE; 0002:P65862; -.
DR PaxDb; P65862; -.
DR EnsemblBacteria; BAB56750; BAB56750; SAV0588.
DR KEGG; sav:SAV0588; -.
DR HOGENOM; CLU_019723_0_1_9; -.
DR OMA; TMLVKMG; -.
DR PhylomeDB; P65862; -.
DR BioCyc; SAUR158878:SAV_RS03260-MON; -.
DR UniPathway; UPA00340; UER00459.
DR Proteomes; UP000002481; 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 3: Inferred from homology;
KW Acyltransferase; Cytoplasm; Transferase.
FT CHAIN 1..328
FT /note="Phosphate acetyltransferase"
FT /id="PRO_0000179141"
SQ SEQUENCE 328 AA; 34952 MW; 7EBE5837CEB3D188 CRC64;
MADLLNVLKD KLSGKNVKIV LPEGEDERVL TAATQLQATD YVTPIVLGDE TKVQSLAQKL
DLDISNIELI NPATSELKAE LVQSFVERRK GKATEEQAQE LLNNVNYFGT MLVYAGKADG
LVSGAAHSTG DTVRPALQII KTKPGVSRTS GIFFMIKGDE QYIFGDCAIN PELDSQGLAE
IAVESAKSAL SFGMDPKVAM LSFSTKGSAK SDDVTKVQEA VKLAQQKAEE EKLEAIIDGE
FQFDAAIVPG VAEKKAPGAK LQGDANVFVF PSLEAGNIGY KIAQRLGGYD AVGPVLQGLN
SPVNDLSRGC SIEDVYNLSI ITAAQALQ