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P08838 (PT1_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphoenolpyruvate-protein phosphotransferase
EC=2.7.3.9
Alternative name(s):
Phosphotransferase system, enzyme I
Gene names
Name:ptsI
Ordered Locus Names:BSU13910
OrganismBacillus subtilis
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length570 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr).

Catalytic activity

Phosphoenolpyruvate + protein L-histidine = pyruvate + protein N(pi)-phospho-L-histidine.

Cofactor

Magnesium By similarity.

Subcellular location

Cytoplasm.

Domain

The N-terminal domain contains the HPr binding site, the central domain the pyrophosphate/phosphate carrier histidine, and the C-terminal domain the pyruvate binding site By similarity.

Miscellaneous

The reaction takes place in three steps, mediated by a phosphocarrier histidine residue located on the surface of the central domain. The two first partial reactions are catalyzed at an active site located on the N-terminal domain, and the third partial reaction is catalyzed at an active site located on the C-terminal domain. For catalytic turnover, the central domain swivels from the concave surface of the N-terminal domain to that of the C-terminal domain By similarity.

Sequence similarities

Belongs to the PEP-utilizing enzyme family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 570570Phosphoenolpyruvate-protein phosphotransferase
PRO_0000147059

Sites

Active site1891Tele-phosphohistidine intermediate By similarity
Active site5021Proton donor By similarity
Metal binding4311Magnesium By similarity
Metal binding4551Magnesium By similarity
Binding site2961Substrate By similarity
Binding site3321Substrate By similarity
Binding site4311Substrate By similarity
Binding site4521Substrate; via carbonyl oxygen By similarity
Binding site4531Substrate; via amide nitrogen By similarity
Binding site4541Substrate By similarity
Binding site4551Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
P08838 [UniParc].

Last modified November 1, 1997. Version 3.
Checksum: 86163CD5639F3369

FASTA57063,079
        10         20         30         40         50         60 
MQELKGIGAS AGIAIAKAYR LEEPDLTVEK KNISDSEAEV SRFDEAIARS KEELEKIKEH 

        70         80         90        100        110        120 
ALKELGQDKA DIFSAHLLVL SDPELLNPVK EKISTDSVNA EFALKETSSM FVTMFESMDN 

       130        140        150        160        170        180 
EYMKERAADI RDVTKRVTGH LLGVEIPNPS MISEEVIIVA EDLTPSDTAQ LNREFVKGFT 

       190        200        210        220        230        240 
TDIGGRTSHS AIMARSLEIP AVVGTKAATG TIQNGVTVIV DGINGDVIID PSAETVKEYE 

       250        260        270        280        290        300 
EKHNAYLAQK AEWAKLVNEP TVSKDGHHVE LAANIGTPDD VKGVLENGGE AVGLYRTEFL 

       310        320        330        340        350        360 
YMGRDQLPTE DEQFDAYKTV LERMEGKSVV VRTLDIGGDK ELPYLQLPKE MNPFLGYRAI 

       370        380        390        400        410        420 
RLCLEEQEIF RTQLRALLRA STYGNLKIMF PMIATVNEFK EAKAILLEEK EKLVKAGQAV 

       430        440        450        460        470        480 
SDDIEVGMMV EIPSTAVIAD QFAKEVDFFS IGTNDLIQYT MAADRMNERV SYLYQPYNPA 

       490        500        510        520        530        540 
ILRLITLVIE AAHKEGKWVG MCGEMAGDEI AIPILLGLGL DEFSMSATSI LPARTQISKL 

       550        560        570 
SKQEAESFKE KILSMSTTEE VVAFVKETFK

« Hide

References

« Hide 'large scale' references
[1]"Sequence analyses and evolutionary relationships among the energy-coupling proteins Enzyme I and HPr of the bacterial phosphoenolpyruvate: sugar phosphotransferase system."
Reizer J., Hoischen C., Reizer A., Pham T.N., Saier M.H. Jr.
Protein Sci. 2:506-521(1993) [PubMed: 7686067] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]Reizer J.
Submitted (MAR-1997) to UniProtKB
Cited for: SEQUENCE REVISION.
[3]"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: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[4]"Detecting and analyzing DNA sequencing errors: toward a higher quality of the Bacillus subtilis genome sequence."
Medigue C., Rose M., Viari A., Danchin A.
Genome Res. 9:1116-1127(1999) [PubMed: 10568751] [Abstract]
Cited for: SEQUENCE REVISION.
[5]"Phosphoenolpyruvate:sugar phosphotransferase system of Bacillus subtilis: nucleotide sequence of ptsX, ptsH and the 5'-end of ptsI and evidence for a ptsHI operon."
Gonzy-Treboul G., Zagorec M., Rain-Guion M.-C., Steinmetz M.
Mol. Microbiol. 3:103-112(1989) [PubMed: 2497294] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-68.
Strain: 168.
[6]"Molecular cloning and characterization of the Bacillus subtilis spore photoproduct lyase (spl) gene, which is involved in repair of UV radiation-induced DNA damage during spore germination."
Fajardo-Cavazos P., Salazar C., Nicholson W.L.
J. Bacteriol. 175:1735-1744(1993) [PubMed: 8449881] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 398-570.
Strain: 168.
[7]"Amino acid sequences of several Bacillus subtilis proteins modified by apparent guanylylation."
Mitchell C., Morris P.W., Vary J.C.
Mol. Microbiol. 6:1579-1581(1992) [PubMed: 1495386] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-13.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M98359 Genomic DNA. Translation: AAB52374.1.
AL009126 Genomic DNA. Translation: CAB13264.2.
X12832 Genomic DNA. Translation: CAA31318.1. Sequence problems.
L08809 Genomic DNA. Translation: AAA22414.1.
PIRC46238.
RefSeqNP_389274.2. NC_000964.3.

3D structure databases

ProteinModelPortalP08838.
SMRP08838. Positions 4-565.
ModBaseSearch...

Protein-protein interaction databases

IntActP08838. 4 interactions.

PTM databases

PhosSiteP08838.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000003054; EBBACP00000003054; EBBACG00000003048.
GeneID939253.
GenomeReviewsGene locus BSU13910 in contig AL009126_GR.
KEGGbsu:BSU13910.
PATRIC18974565. VBIBacSub10457_1474.

Organism-specific databases

GenoListBSU13910. [Micado]

Phylogenomic databases

GeneTreeEBGT00050000002837.
HOGENOMHBG456539.
OMAIFSAHLL.
PhylomeDBP08838.
ProtClustDBCLSK928129.

Enzyme and pathway databases

BioCycBSUB:BSU13910-MONOMER.
BRENDA2.7.3.9. 700.

Family and domain databases

InterProIPR008279. PEP-util_enz_mobile_dom.
IPR018274. PEP_util_AS.
IPR000121. PEP_util_C.
IPR023151. PEP_util_CS.
IPR006318. PEP_util_enz.
IPR024692. PTS_enz_I.
IPR008731. PTS_PEP_utilis_N.
IPR015813. Pyrv/PenolPyrv_Kinase.
[Graphical view]
Gene3DG3DSA:3.50.30.10. PEP_mobile. 1 hit.
G3DSA:1.10.274.10. PTS_PEP_utilis_N. 1 hit.
G3DSA:3.20.20.60. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
KOK08483.
PANTHERPTHR22931:SF10. PTHR22931:SF10. 1 hit.
PfamPF05524. PEP-utilisers_N. 1 hit.
PF00391. PEP-utilizers. 1 hit.
PF02896. PEP-utilizers_C. 1 hit.
[Graphical view]
PIRSFPIRSF000732. PTS_enzyme_I. 1 hit.
PRINTSPR01736. PHPHTRNFRASE.
SUPFAMSSF47831. PEP-utilisers_N. 1 hit.
SSF52009. PEP_mobile. 1 hit.
SSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
TIGRFAMsTIGR01417. PTS_I_fam. 1 hit.
PROSITEPS00742. PEP_ENZYMES_2. 1 hit.
PS00370. PEP_ENZYMES_PHOS_SITE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePT1_BACSU
AccessionPrimary (citable) accession number: P08838
Secondary accession number(s): O31692
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1997
Last modified: January 25, 2012
This is version 102 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents