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P39646 (PTAS_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphate acetyltransferase

EC=2.3.1.8
Alternative name(s):
Phosphotransacetylase
Vegetative protein 43
Short name=VEG43
Gene names
Name:pta
Synonyms:ywfJ
Ordered Locus Names:BSU37660
ORF Names:ipa-88d
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length323 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Acetyl-CoA + phosphate = CoA + acetyl phosphate.

Pathway

Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 2/2.

Subcellular location

Cytoplasm Potential.

Sequence similarities

Belongs to the phosphate acetyltransferase and butyryltransferase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionAcyltransferase
Transferase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processacetyl-CoA biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionphosphate acetyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 323322Phosphate acetyltransferase
PRO_0000179120

Secondary structure

............................................................. 323
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P39646 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 7F4A56981C151AF6

FASTA32334,791
        10         20         30         40         50         60 
MADLFSTVQE KVAGKDVKIV FPEGLDERIL EAVSKLAGNK VLNPIVIGNE NEIQAKAKEL 

        70         80         90        100        110        120 
NLTLGGVKIY DPHTYEGMED LVQAFVERRK GKATEEQARK ALLDENYFGT MLVYKGLADG 

       130        140        150        160        170        180 
LVSGAAHSTA DTVRPALQII KTKEGVKKTS GVFIMARGEE QYVFADCAIN IAPDSQDLAE 

       190        200        210        220        230        240 
IAIESANTAK MFDIEPRVAM LSFSTKGSAK SDETEKVADA VKIAKEKAPE LTLDGEFQFD 

       250        260        270        280        290        300 
AAFVPSVAEK KAPDSEIKGD ANVFVFPSLE AGNIGYKIAQ RLGNFEAVGP ILQGLNMPVN 

       310        320 
DLSRGCNAED VYNLALITAA QAL 

« Hide

References

« Hide 'large scale' references
[1]"Bacillus subtilis genome project: cloning and sequencing of the 97 kb region from 325 degrees to 333 degrees."
Glaser P., Kunst F., Arnaud M., Coudart M.P., Gonzales W., Hullo M.-F., Ionescu M., Lubochinsky B., Marcelino L., Moszer I., Presecan E., Santana M., Schneider E., Schweizer J., Vertes A., Rapoport G., Danchin A.
Mol. Microbiol. 10:371-384(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[3]"First steps from a two-dimensional protein index towards a response-regulation map for Bacillus subtilis."
Antelmann H., Bernhardt J., Schmid R., Mach H., Voelker U., Hecker M.
Electrophoresis 18:1451-1463(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-11.
Strain: 168 / IS58.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X73124 Genomic DNA. Translation: CAA51644.1.
AL009126 Genomic DNA. Translation: CAB15793.1.
PIRS39743.
RefSeqNP_391646.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1TD9X-ray2.75A/B/C/D/E/F2-322[»]
1XCOX-ray2.85A/B/C/D/E/F2-322[»]
ProteinModelPortalP39646.
SMRP39646. Positions 1-323.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU37660.

PTM databases

PhosSiteP0802233.

Proteomic databases

PaxDbP39646.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB15793; CAB15793; BSU37660.
GeneID936581.
KEGGbsu:BSU37660.
PATRIC18979570. VBIBacSub10457_3947.

Organism-specific databases

GenoListBSU37660. [Micado]

Phylogenomic databases

eggNOGCOG0280.
HOGENOMHOG000053796.
KOK00625.
OMAGVFIMAR.
OrthoDBEOG6BKJ5W.
ProtClustDBPRK09653.

Enzyme and pathway databases

BioCycBSUB:BSU37660-MONOMER.
UniPathwayUPA00340; UER00459.

Family and domain databases

InterProIPR012147. P_Ac_Bu_trans.
IPR004614. P_AcTrfase.
IPR002505. PTA_PTB.
[Graphical view]
PfamPF01515. PTA_PTB. 1 hit.
[Graphical view]
PIRSFPIRSF000428. P_Ac_trans. 1 hit.
TIGRFAMsTIGR00651. pta. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP39646.

Entry information

Entry namePTAS_BACSU
AccessionPrimary (citable) accession number: P39646
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 23, 2007
Last modified: November 13, 2013
This is version 105 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList