ID   PTA_BUCAP               Reviewed;         709 AA.
AC   Q8K9W5;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Phosphate acetyltransferase;
DE            EC=2.3.1.8;
DE   AltName: Full=Phosphotransacetylase;
GN   Name=pta; OrderedLocusNames=BUsg_170;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
CC   -!- FUNCTION: Involved in acetate metabolism. {ECO:0000250}.
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   -!- SUBUNIT: Homohexamer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- DOMAIN: The N-terminal region seems to be important for proper
CC       quaternary structure. The C-terminal region contains the substrate-
CC       binding site (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the CobB/CobQ family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the phosphate
CC       acetyltransferase and butyryltransferase family. {ECO:0000305}.
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DR   EMBL; AE013218; AAM67737.1; -; Genomic_DNA.
DR   RefSeq; WP_011053704.1; NC_004061.1.
DR   AlphaFoldDB; Q8K9W5; -.
DR   SMR; Q8K9W5; -.
DR   STRING; 198804.BUsg_170; -.
DR   EnsemblBacteria; AAM67737; AAM67737; BUsg_170.
DR   KEGG; bas:BUsg_170; -.
DR   eggNOG; COG0280; Bacteria.
DR   eggNOG; COG0857; Bacteria.
DR   HOGENOM; CLU_019723_2_1_6; -.
DR   OMA; YSIANDN; -.
DR   OrthoDB; 1301815at2; -.
DR   UniPathway; UPA00340; UER00459.
DR   Proteomes; UP000000416; 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; 3.40.1390.20; -; 1.
DR   Gene3D; 3.40.50.10750; -; 1.
DR   Gene3D; 3.40.50.10950; -; 1.
DR   InterPro; IPR010766; DRTGG.
DR   InterPro; IPR016475; P-Actrans_bac.
DR   InterPro; IPR004614; P_AcTrfase.
DR   InterPro; IPR042113; P_AcTrfase_dom1.
DR   InterPro; IPR042112; P_AcTrfase_dom2.
DR   InterPro; IPR002505; PTA_PTB.
DR   InterPro; IPR028979; Ser_kin/Pase_Hpr-like_N_sf.
DR   Pfam; PF07085; DRTGG; 1.
DR   Pfam; PF01515; PTA_PTB; 1.
DR   PIRSF; PIRSF006107; PhpActrans_proteobac; 1.
DR   SUPFAM; SSF75138; SSF75138; 1.
DR   TIGRFAMs; TIGR00651; pta; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cytoplasm; Transferase.
FT   CHAIN           1..709
FT                   /note="Phosphate acetyltransferase"
FT                   /id="PRO_0000179123"
FT   REGION          389..709
FT                   /note="Phosphate acetyltransferase"
SQ   SEQUENCE   709 AA;  81236 MW;  DF21DF13C0FC3FB7 CRC64;
     MSRIIMLIPL NKKVSLTTIS LSILYFFNKK EQKNCFKSFS YLPLIKSDNI NFIRAYFSKK
     INVLDDINFF KKNFNSDEYS YLLDKIIKEC FNKKKINEFI LIKGISRKEH DDADQINFDI
     AQNIDAEVIF IDNLKDFSLG CFKRKERKIN VFLQQKKYKN FLGLIFSDIN SPFIFNKMKY
     NFFDKLIILK NTKKNTCIHA IKKNIFFNSF FRVIAFIPWN KKLVKSSVIN IFKFLNATLV
     NTISIKDAFI KNITIFDEDS SVILKKSYAN TLVLISSSRM ETFFKTLYLV CKSKKIGAIL
     LTGVLKLSEN SIKLLKFLTN QGVPVFFIKE NTVETLSQLQ KFNFNINVQN KYFINKLLEY
     TSSFFNKNHL ISLKKKTTNF YKKTYSPKEF CYRLKILSKS KHKRIILPES YEPRILKAAS
     ICHRLGIAEC ILLGDPKKIY NIANENKIDL NKNIEIKDPI LIRDQYVPRL LEIRKNKKID
     EIFARKQLKD NVILATLILE SGKVDGLVSG TINTTANTIR PALQIIKTDP IYSLVSSIFF
     ILLPNEVLIY GDCAINIEPN SKELAEIAIQ SANSAKMFGI EPRIAMLSYS TGFSGTGWQV
     EKIRDATSIV KSKRPDLLID GPIQYDAAIS KEVAKLKIPY SSILGSANIF IFPDLNSGNI
     TYKAVQRSAD LICIGPMLQG LKKPVNDLSR GASVEDIVYT IALTSIQSL