ID   PTAS_RICPR              Reviewed;         351 AA.
AC   Q9ZE39;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   27-MAR-2024, entry version 96.
DE   RecName: Full=Phosphate acetyltransferase;
DE            EC=2.3.1.8;
DE   AltName: Full=Phosphotransacetylase;
GN   Name=pta; OrderedLocusNames=RP109;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
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; AJ235270; CAA14578.1; -; Genomic_DNA.
DR   PIR; C71720; C71720.
DR   RefSeq; NP_220501.1; NC_000963.1.
DR   RefSeq; WP_004597142.1; NC_000963.1.
DR   AlphaFoldDB; Q9ZE39; -.
DR   SMR; Q9ZE39; -.
DR   STRING; 272947.gene:17555192; -.
DR   EnsemblBacteria; CAA14578; CAA14578; CAA14578.
DR   GeneID; 57569237; -.
DR   KEGG; rpr:RP109; -.
DR   PATRIC; fig|272947.5.peg.111; -.
DR   eggNOG; COG0280; Bacteria.
DR   HOGENOM; CLU_056531_1_0_5; -.
DR   OrthoDB; 9800237at2; -.
DR   UniPathway; UPA00340; UER00459.
DR   Proteomes; UP000002480; 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; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR   InterPro; IPR012147; P_Ac_Bu_trans.
DR   InterPro; IPR002505; PTA_PTB.
DR   PANTHER; PTHR43356; PHOSPHATE ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR43356:SF2; PHOSPHATE ACETYLTRANSFERASE; 1.
DR   Pfam; PF01515; PTA_PTB; 1.
DR   PIRSF; PIRSF000428; P_Ac_trans; 1.
DR   SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT   CHAIN           1..351
FT                   /note="Phosphate acetyltransferase"
FT                   /id="PRO_0000179138"
SQ   SEQUENCE   351 AA;  38170 MW;  2713B57086B49369 CRC64;
     MKKQHIINET FLDEILAQKL GTTYIPPTEI KDSDFDKAAK HFINLLLRAD GLKPIKTAVV
     HPIDKESLLG AVRAAQFNVI KPILIGPQHK IESVAKVNDV DLENYQVINA EHSHEAAKKA
     VELAKKREVA AIMKGALHTD ELMSAVVYKE NGLRTERRIS HAFLMAVATF PKPFIITDAA
     INIRPTLEDK RDIVQNAIDL MHIIKEDKQV RVAVLSAVET VTSAIPTTLD AAALSKMADR
     GQITNAVVDG PLAFDNAISL FAAEAKGISS PVSGNADILV VPDLESGNML AKQLKYLGQA
     VMAGIVLGAR VPIILTSRAD PIDMRVISCV LASFIYNQTK AKLHNSSKSI I
//