PTAS_BACSU
ID PTAS_BACSU Reviewed; 323 AA.
AC P39646;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Phosphate acetyltransferase;
DE EC=2.3.1.8;
DE AltName: Full=Phosphotransacetylase;
DE AltName: Full=Vegetative protein 43;
DE Short=VEG43;
GN Name=pta; Synonyms=ywfJ; OrderedLocusNames=BSU37660; ORFNames=ipa-88d;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7934828; DOI=10.1111/j.1365-2958.1993.tb01963.x;
RA Glaser P., Kunst F., Arnaud M., Coudart M.P., Gonzales W., Hullo M.-F.,
RA Ionescu M., Lubochinsky B., Marcelino L., Moszer I., Presecan E.,
RA Santana M., Schneider E., Schweizer J., Vertes A., Rapoport G., Danchin A.;
RT "Bacillus subtilis genome project: cloning and sequencing of the 97 kb
RT region from 325 degrees to 333 degrees.";
RL Mol. Microbiol. 10:371-384(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP PROTEIN SEQUENCE OF 2-11.
RC STRAIN=168 / IS58;
RX PubMed=9298659; DOI=10.1002/elps.1150180820;
RA Antelmann H., Bernhardt J., Schmid R., Mach H., Voelker U., Hecker M.;
RT "First steps from a two-dimensional protein index towards a response-
RT regulation map for Bacillus subtilis.";
RL Electrophoresis 18:1451-1463(1997).
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; X73124; CAA51644.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15793.1; -; Genomic_DNA.
DR PIR; S39743; S39743.
DR RefSeq; NP_391646.1; NC_000964.3.
DR RefSeq; WP_003243393.1; NZ_JNCM01000034.1.
DR PDB; 1TD9; X-ray; 2.75 A; A/B/C/D/E/F=1-323.
DR PDB; 1XCO; X-ray; 2.85 A; A/B/C/D/E/F=1-323.
DR PDBsum; 1TD9; -.
DR PDBsum; 1XCO; -.
DR AlphaFoldDB; P39646; -.
DR SMR; P39646; -.
DR STRING; 224308.BSU37660; -.
DR DrugBank; DB02897; Acetylphosphate.
DR jPOST; P39646; -.
DR PaxDb; P39646; -.
DR PRIDE; P39646; -.
DR EnsemblBacteria; CAB15793; CAB15793; BSU_37660.
DR GeneID; 936581; -.
DR KEGG; bsu:BSU37660; -.
DR PATRIC; fig|224308.179.peg.4078; -.
DR eggNOG; COG0280; Bacteria.
DR InParanoid; P39646; -.
DR OMA; TMLVKMG; -.
DR PhylomeDB; P39646; -.
DR BioCyc; BSUB:BSU37660-MON; -.
DR UniPathway; UPA00340; UER00459.
DR EvolutionaryTrace; P39646; -.
DR Proteomes; UP000001570; 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 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Cytoplasm; Direct protein sequencing;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298659"
FT CHAIN 2..323
FT /note="Phosphate acetyltransferase"
FT /id="PRO_0000179120"
FT HELIX 2..12
FT /evidence="ECO:0007829|PDB:1TD9"
FT STRAND 18..22
FT /evidence="ECO:0007829|PDB:1TD9"
FT HELIX 27..38
FT /evidence="ECO:0007829|PDB:1TD9"
FT STRAND 41..48
FT /evidence="ECO:0007829|PDB:1TD9"
FT HELIX 50..58
FT /evidence="ECO:0007829|PDB:1TD9"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:1TD9"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:1TD9"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:1TD9"
FT HELIX 78..88
FT /evidence="ECO:0007829|PDB:1TD9"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:1TD9"
FT HELIX 95..101
FT /evidence="ECO:0007829|PDB:1TD9"
FT HELIX 105..114
FT /evidence="ECO:0007829|PDB:1TD9"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:1TD9"
FT HELIX 129..138
FT /evidence="ECO:0007829|PDB:1TD9"
FT STRAND 150..157
FT /evidence="ECO:0007829|PDB:1TD9"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:1TD9"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:1TD9"
FT HELIX 175..190
FT /evidence="ECO:0007829|PDB:1TD9"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:1TD9"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:1TD9"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:1TD9"
FT HELIX 212..227
FT /evidence="ECO:0007829|PDB:1TD9"
FT STRAND 233..237
FT /evidence="ECO:0007829|PDB:1TD9"
FT HELIX 239..243
FT /evidence="ECO:0007829|PDB:1TD9"
FT HELIX 245..251
FT /evidence="ECO:0007829|PDB:1TD9"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:1XCO"
FT STRAND 262..265
FT /evidence="ECO:0007829|PDB:1TD9"
FT HELIX 269..281
FT /evidence="ECO:0007829|PDB:1TD9"
FT TURN 282..284
FT /evidence="ECO:0007829|PDB:1TD9"
FT STRAND 286..297
FT /evidence="ECO:0007829|PDB:1TD9"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:1TD9"
FT HELIX 308..322
FT /evidence="ECO:0007829|PDB:1TD9"
SQ SEQUENCE 323 AA; 34791 MW; 7F4A56981C151AF6 CRC64;
MADLFSTVQE KVAGKDVKIV FPEGLDERIL EAVSKLAGNK VLNPIVIGNE NEIQAKAKEL
NLTLGGVKIY DPHTYEGMED LVQAFVERRK GKATEEQARK ALLDENYFGT MLVYKGLADG
LVSGAAHSTA DTVRPALQII KTKEGVKKTS GVFIMARGEE QYVFADCAIN IAPDSQDLAE
IAIESANTAK MFDIEPRVAM LSFSTKGSAK SDETEKVADA VKIAKEKAPE LTLDGEFQFD
AAFVPSVAEK KAPDSEIKGD ANVFVFPSLE AGNIGYKIAQ RLGNFEAVGP ILQGLNMPVN
DLSRGCNAED VYNLALITAA QAL
