ID   PTA_MYCTU               Reviewed;         690 AA.
AC   P9WHP1; L0T5A1; P96254;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 39.
DE   RecName: Full=Phosphate acetyltransferase;
DE            EC=2.3.1.8;
DE   AltName: Full=Phosphotransacetylase;
GN   Name=pta; OrderedLocusNames=Rv0408; ORFNames=MTCY22G10.04;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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   -!- 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; AL123456; CCP43139.1; -; Genomic_DNA.
DR   PIR; F70628; F70628.
DR   RefSeq; NP_214922.1; NC_000962.3.
DR   RefSeq; WP_003898439.1; NZ_NVQJ01000002.1.
DR   AlphaFoldDB; P9WHP1; -.
DR   SMR; P9WHP1; -.
DR   STRING; 83332.Rv0408; -.
DR   PaxDb; P9WHP1; -.
DR   DNASU; 886401; -.
DR   GeneID; 886401; -.
DR   KEGG; mtu:Rv0408; -.
DR   TubercuList; Rv0408; -.
DR   eggNOG; COG0280; Bacteria.
DR   eggNOG; COG0857; Bacteria.
DR   OMA; FFMCLAD; -.
DR   PhylomeDB; P9WHP1; -.
DR   UniPathway; UPA00340; UER00459.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; HDA:MTBBASE.
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   1: Evidence at protein level;
KW   Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT   CHAIN           1..690
FT                   /note="Phosphate acetyltransferase"
FT                   /id="PRO_0000179135"
FT   REGION          365..690
FT                   /note="Phosphate acetyltransferase"
SQ   SEQUENCE   690 AA;  72949 MW;  C01C412AF2810CCE CRC64;
     MADSSAIYLA APESQTGKST IALGLLHRLT AMVAKVGVFR PITRLSAERD YILELLLAHT
     SAGLPYERCV GVTYQQLHAD RDDAIAEIVD SYHAMADECD AVVVVGSDYT DVTSPTELSV
     NGRIAVNLGA PVLLTVRAKD RTPDQVASVV EVCLAELDTQ RAHTAAVVAN RCELSAIPAV
     TDALRRFTPP SYVVPEEPLL SAPTVAELTQ AVNGAVVSGD VALREREVMG VLAAGMTADH
     VLERLTDGMA VITPGDRSDV VLAVASAHAA EGFPSLSCIV LNGGFQLHPA IAALVSGLRL
     RLPVIATALG TYDTASAAAS ARGLVTATSQ RKIDTALELM DRHVDVAGLL AQLTIPIPTV
     TTPQMFTYRL LQQARSDLMR IVLPEGDDDR ILKSAGRLLQ RGIVDLTILG DEAKVRLRAA
     ELGVDLDGAT VIEPCASELH DQFADQYAQL RKAKGITVEH AREIMNDATY FGTMLVHNCH
     ADGMVSGAAH TTAHTVRPAL EIIKTVPGIS TVSSIFLMCL PDRVLAYGDC AIIPNPTVEQ
     LADIAICSAR TAAQFGIEPR VAMLSYSTGD SGKGADVDKV RAATELVRAR EPQLPVEGPI
     QYDAAVEPSV AATKLRDSPV AGRATVLIFP DLNTGNNTYK AVQRSAGAIA IGPVLQGLRK
     PVNDLSRGAL VDDIVNTVAI TAIQAQGVHE