ID   PTA_STRCO               Reviewed;         697 AA.
AC   Q8CJR5;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Phosphate acetyltransferase;
DE            EC=2.3.1.8;
DE   AltName: Full=Phosphotransacetylase;
GN   Name=pta; OrderedLocusNames=SCO5425; ORFNames=SC6A11.01c, SC8F4.29c;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(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; AL939123; CAD55352.1; -; Genomic_DNA.
DR   RefSeq; NP_733663.1; NC_003888.3.
DR   RefSeq; WP_011030239.1; NZ_VNID01000011.1.
DR   AlphaFoldDB; Q8CJR5; -.
DR   SMR; Q8CJR5; -.
DR   STRING; 100226.SCO5425; -.
DR   GeneID; 1100865; -.
DR   KEGG; sco:SCO5425; -.
DR   PATRIC; fig|100226.15.peg.5506; -.
DR   eggNOG; COG0280; Bacteria.
DR   eggNOG; COG0857; Bacteria.
DR   HOGENOM; CLU_019723_3_0_11; -.
DR   InParanoid; Q8CJR5; -.
DR   OMA; FFMCLAD; -.
DR   PhylomeDB; Q8CJR5; -.
DR   UniPathway; UPA00340; UER00459.
DR   Proteomes; UP000001973; 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   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR010766; DRTGG.
DR   InterPro; IPR016475; P-Actrans_bac.
DR   InterPro; IPR027417; P-loop_NTPase.
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; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF75138; SSF75138; 1.
DR   TIGRFAMs; TIGR00651; pta; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT   CHAIN           1..697
FT                   /note="Phosphate acetyltransferase"
FT                   /id="PRO_0000405553"
FT   REGION          366..697
FT                   /note="Phosphate acetyltransferase"
SQ   SEQUENCE   697 AA;  74047 MW;  D52002198968B71E CRC64;
     MTRSVYVTGI DRGDGRQVVE LGVMELLTRQ VDRVGVFRPL VHDGPDRLFE LLRARYRLSQ
     DPATVYGMDY QEASLLQAEQ GVDELVSALV DRFHLVARDY DVVLVLGTDY ADTQFPDELS
     LNARLANEFG ASVLPVVGGR KQTADSVLAE THNAFRAYDG LGCDVLAMVT NRVAREDRDE
     IAERLAHRLP VPCWVVPDEP ALSAPTVSQI AHALGAEIVL GDDSGLARDA LDFVFGGAML
     PNLLAALTPG CLVITPGDRA DLVIGTLAAH SAGTPPIAGV LLTLNEVPGE GILTLAARLA
     PGTPVLSVTG TSFPTAERLF SLEGKLGAAT PRKAETALGL FERYVDTAEL NKRVSAPSSD
     RVTPMMFEHK LLEQARSDLR RVVLPEGTEE RVLHAAEVLL RRGVCELTLL GPVEQIRKKA
     ADLGIDLGGA ELIDPAASEL RDSFAEKYAA LRAHKGVTVE LAYDVVSDVN YFGTLMVQEG
     FADGMVSGSV HSTAATIRPA FEIIKTKPDA AIVSSVFFMC LADKVLVYGD CAVNPDPDAE
     QLADIATQSA STAAQFGVEP RIAMLSYSTG TSGSGADVDK VREATELVRS RRPDLSVEGP
     IQYDAAVEPS VAATKLPGSA VAGQASVLIF PDLNTGNNTY KAVQRSAGAI AVGPVLQGLR
     KPVNDLSRGA LVQDIVNTVA ITAIQAQQSP TEKASAQ