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Protein

Phosphoenolpyruvate-protein phosphotransferase

Gene

ptsI

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).1 Publication

Catalytic activityi

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

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei189 – 1891Tele-phosphohistidine intermediate1 Publication
Binding sitei296 – 2961SubstrateBy similarity
Binding sitei332 – 3321Substrate
Metal bindingi431 – 4311Magnesium
Binding sitei431 – 4311SubstrateBy similarity
Binding sitei452 – 4521Substrate; via carbonyl oxygenBy similarity
Binding sitei453 – 4531Substrate; via amide nitrogenBy similarity
Binding sitei454 – 4541Substrate; via amide nitrogen
Metal bindingi455 – 4551Magnesium
Binding sitei455 – 4551Substrate; via amide nitrogen
Active sitei502 – 5021Proton donor1 Publication

GO - Molecular functioni

  • kinase activity Source: UniProtKB-KW
  • magnesium ion binding Source: EcoCyc
  • metal ion binding Source: EcoCyc
  • phosphoenolpyruvate-protein phosphotransferase activity Source: EcoCyc

GO - Biological processi

  • phosphoenolpyruvate-dependent sugar phosphotransferase system Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Phosphotransferase system, Sugar transport, Transport

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:PTSI-MONOMER.
ECOL316407:JW2409-MONOMER.
BRENDAi2.7.3.9. 2026.
SABIO-RKP08839.

Protein family/group databases

TCDBi8.A.7.1.1. the phosphotransferase system enzyme i (ei) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoenolpyruvate-protein phosphotransferase (EC:2.7.3.9)
Alternative name(s):
Phosphotransferase system, enzyme I
Gene namesi
Name:ptsI
Ordered Locus Names:b2416, JW2409
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10789. ptsI.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • phosphoenolpyruvate-dependent sugar phosphotransferase complex Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 575575Phosphoenolpyruvate-protein phosphotransferasePRO_0000147067Add
BLAST

Proteomic databases

EPDiP08839.
PaxDbiP08839.
PRIDEiP08839.

2D gel databases

SWISS-2DPAGEP08839.

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
bglGP119893EBI-551533,EBI-545674
ptsHP0AA042EBI-551533,EBI-902853

Protein-protein interaction databases

BioGridi4260570. 498 interactions.
851219. 1 interaction.
DIPiDIP-10603N.
IntActiP08839. 14 interactions.
MINTiMINT-5290328.
STRINGi511145.b2416.

Structurei

Secondary structure

1
575
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 84Combined sources
Beta strandi12 – 187Combined sources
Turni33 – 353Combined sources
Helixi36 – 6530Combined sources
Helixi67 – 8014Combined sources
Helixi83 – 9614Combined sources
Helixi100 – 11213Combined sources
Turni113 – 1153Combined sources
Beta strandi116 – 1183Combined sources
Helixi121 – 14222Combined sources
Helixi149 – 1513Combined sources
Beta strandi156 – 1594Combined sources
Helixi165 – 1706Combined sources
Helixi173 – 1753Combined sources
Beta strandi176 – 1805Combined sources
Beta strandi183 – 1853Combined sources
Beta strandi186 – 1883Combined sources
Helixi189 – 1979Combined sources
Beta strandi201 – 2033Combined sources
Helixi208 – 2114Combined sources
Beta strandi217 – 2204Combined sources
Turni222 – 2254Combined sources
Beta strandi227 – 2304Combined sources
Helixi233 – 2397Combined sources
Turni240 – 2434Combined sources
Helixi244 – 2474Combined sources
Helixi254 – 2563Combined sources
Beta strandi270 – 2778Combined sources
Helixi279 – 2868Combined sources
Beta strandi290 – 2967Combined sources
Helixi297 – 3015Combined sources
Beta strandi304 – 3063Combined sources
Helixi310 – 32314Combined sources
Turni324 – 3263Combined sources
Beta strandi329 – 3324Combined sources
Beta strandi337 – 3393Combined sources
Helixi343 – 3453Combined sources
Helixi353 – 3553Combined sources
Helixi360 – 3634Combined sources
Helixi367 – 38014Combined sources
Beta strandi386 – 3927Combined sources
Helixi396 – 41520Combined sources
Beta strandi425 – 4306Combined sources
Helixi433 – 4375Combined sources
Helixi439 – 4435Combined sources
Beta strandi447 – 4515Combined sources
Helixi453 – 4619Combined sources
Helixi468 – 4736Combined sources
Beta strandi476 – 4783Combined sources
Helixi479 – 49416Combined sources
Beta strandi498 – 5014Combined sources
Turni504 – 5074Combined sources
Turni509 – 5113Combined sources
Helixi512 – 5176Combined sources
Beta strandi522 – 5254Combined sources
Helixi527 – 5293Combined sources
Helixi530 – 5389Combined sources
Helixi542 – 55413Combined sources
Helixi558 – 57215Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EZANMR-A1-258[»]
1EZBNMR-A1-258[»]
1EZCNMR-A1-258[»]
1EZDNMR-A1-258[»]
1ZYMX-ray2.50A/B1-258[»]
2EZANMR-A1-258[»]
2EZBNMR-A1-258[»]
2EZCNMR-A1-258[»]
2HWGX-ray2.70A/B1-575[»]
2KX9Other-A/B1-573[»]
2L5HOther-A/B1-573[»]
2MP0NMR-A1-258[»]
2N5TOther-A/B1-575[»]
2XDFOther-A/B1-573[»]
3EZANMR-A1-249[»]
3EZBNMR-A1-258[»]
3EZENMR-A1-258[»]
ProteinModelPortaliP08839.
SMRiP08839. Positions 1-573.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08839.

Family & Domainsi

Domaini

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.

Sequence similaritiesi

Belongs to the PEP-utilizing enzyme family.Curated

Phylogenomic databases

eggNOGiENOG4105BZ3. Bacteria.
COG1080. LUCA.
HOGENOMiHOG000278513.
InParanoidiP08839.
KOiK08483.
OMAiDYVLGFA.
OrthoDBiEOG657JBQ.
PhylomeDBiP08839.

Family and domain databases

Gene3Di1.10.274.10. 1 hit.
3.20.20.60. 1 hit.
3.50.30.10. 1 hit.
InterProiIPR008279. PEP-util_enz_mobile_dom.
IPR018274. PEP_util_AS.
IPR000121. PEP_util_C.
IPR023151. PEP_util_CS.
IPR024692. PTS_EI.
IPR006318. PTS_EI-like.
IPR008731. PTS_EIN.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
PfamiPF05524. PEP-utilisers_N. 1 hit.
PF00391. PEP-utilizers. 1 hit.
PF02896. PEP-utilizers_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000732. PTS_enzyme_I. 1 hit.
SUPFAMiSSF47831. SSF47831. 1 hit.
SSF51621. SSF51621. 1 hit.
SSF52009. SSF52009. 1 hit.
TIGRFAMsiTIGR01417. PTS_I_fam. 1 hit.
PROSITEiPS00742. PEP_ENZYMES_2. 1 hit.
PS00370. PEP_ENZYMES_PHOS_SITE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P08839-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MISGILASPG IAFGKALLLK EDEIVIDRKK ISADQVDQEV ERFLSGRAKA
60 70 80 90 100
SAQLETIKTK AGETFGEEKE AIFEGHIMLL EDEELEQEII ALIKDKHMTA
110 120 130 140 150
DAAAHEVIEG QASALEELDD EYLKERAADV RDIGKRLLRN ILGLKIIDLS
160 170 180 190 200
AIQDEVILVA ADLTPSETAQ LNLKKVLGFI TDAGGRTSHT SIMARSLELP
210 220 230 240 250
AIVGTGSVTS QVKNDDYLIL DAVNNQVYVN PTNEVIDKMR AVQEQVASEK
260 270 280 290 300
AELAKLKDLP AITLDGHQVE VCANIGTVRD VEGAERNGAE GVGLYRTEFL
310 320 330 340 350
FMDRDALPTE EEQFAAYKAV AEACGSQAVI VRTMDIGGDK ELPYMNFPKE
360 370 380 390 400
ENPFLGWRAI RIAMDRREIL RDQLRAILRA SAFGKLRIMF PMIISVEEVR
410 420 430 440 450
ALRKEIEIYK QELRDEGKAF DESIEIGVMV ETPAAATIAR HLAKEVDFFS
460 470 480 490 500
IGTNDLTQYT LAVDRGNDMI SHLYQPMSPS VLNLIKQVID ASHAEGKWTG
510 520 530 540 550
MCGELAGDER ATLLLLGMGL DEFSMSAISI PRIKKIIRNT NFEDAKVLAE
560 570
QALAQPTTDE LMTLVNKFIE EKTIC
Length:575
Mass (Da):63,562
Last modified:November 1, 1988 - v1
Checksum:i4278F0838855E950
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02796 Genomic DNA. Translation: AAA24441.1.
M10425 Genomic DNA. Translation: AAA24439.1.
U00096 Genomic DNA. Translation: AAC75469.1.
AP009048 Genomic DNA. Translation: BAA16290.1.
M21994 Genomic DNA. Translation: AAA24385.1.
M21451 Genomic DNA. Translation: AAA23656.1.
PIRiB29785. WQECPI.
RefSeqiNP_416911.1. NC_000913.3.
WP_000623140.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75469; AAC75469; b2416.
BAA16290; BAA16290; BAA16290.
GeneIDi946879.
KEGGiecj:JW2409.
eco:b2416.
PATRICi32120215. VBIEscCol129921_2510.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02796 Genomic DNA. Translation: AAA24441.1.
M10425 Genomic DNA. Translation: AAA24439.1.
U00096 Genomic DNA. Translation: AAC75469.1.
AP009048 Genomic DNA. Translation: BAA16290.1.
M21994 Genomic DNA. Translation: AAA24385.1.
M21451 Genomic DNA. Translation: AAA23656.1.
PIRiB29785. WQECPI.
RefSeqiNP_416911.1. NC_000913.3.
WP_000623140.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EZANMR-A1-258[»]
1EZBNMR-A1-258[»]
1EZCNMR-A1-258[»]
1EZDNMR-A1-258[»]
1ZYMX-ray2.50A/B1-258[»]
2EZANMR-A1-258[»]
2EZBNMR-A1-258[»]
2EZCNMR-A1-258[»]
2HWGX-ray2.70A/B1-575[»]
2KX9Other-A/B1-573[»]
2L5HOther-A/B1-573[»]
2MP0NMR-A1-258[»]
2N5TOther-A/B1-575[»]
2XDFOther-A/B1-573[»]
3EZANMR-A1-249[»]
3EZBNMR-A1-258[»]
3EZENMR-A1-258[»]
ProteinModelPortaliP08839.
SMRiP08839. Positions 1-573.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260570. 498 interactions.
851219. 1 interaction.
DIPiDIP-10603N.
IntActiP08839. 14 interactions.
MINTiMINT-5290328.
STRINGi511145.b2416.

Protein family/group databases

TCDBi8.A.7.1.1. the phosphotransferase system enzyme i (ei) family.

2D gel databases

SWISS-2DPAGEP08839.

Proteomic databases

EPDiP08839.
PaxDbiP08839.
PRIDEiP08839.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75469; AAC75469; b2416.
BAA16290; BAA16290; BAA16290.
GeneIDi946879.
KEGGiecj:JW2409.
eco:b2416.
PATRICi32120215. VBIEscCol129921_2510.

Organism-specific databases

EchoBASEiEB0782.
EcoGeneiEG10789. ptsI.

Phylogenomic databases

eggNOGiENOG4105BZ3. Bacteria.
COG1080. LUCA.
HOGENOMiHOG000278513.
InParanoidiP08839.
KOiK08483.
OMAiDYVLGFA.
OrthoDBiEOG657JBQ.
PhylomeDBiP08839.

Enzyme and pathway databases

BioCyciEcoCyc:PTSI-MONOMER.
ECOL316407:JW2409-MONOMER.
BRENDAi2.7.3.9. 2026.
SABIO-RKP08839.

Miscellaneous databases

EvolutionaryTraceiP08839.
PROiP08839.

Family and domain databases

Gene3Di1.10.274.10. 1 hit.
3.20.20.60. 1 hit.
3.50.30.10. 1 hit.
InterProiIPR008279. PEP-util_enz_mobile_dom.
IPR018274. PEP_util_AS.
IPR000121. PEP_util_C.
IPR023151. PEP_util_CS.
IPR024692. PTS_EI.
IPR006318. PTS_EI-like.
IPR008731. PTS_EIN.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
PfamiPF05524. PEP-utilisers_N. 1 hit.
PF00391. PEP-utilizers. 1 hit.
PF02896. PEP-utilizers_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000732. PTS_enzyme_I. 1 hit.
SUPFAMiSSF47831. SSF47831. 1 hit.
SSF51621. SSF51621. 1 hit.
SSF52009. SSF52009. 1 hit.
TIGRFAMsiTIGR01417. PTS_I_fam. 1 hit.
PROSITEiPS00742. PEP_ENZYMES_2. 1 hit.
PS00370. PEP_ENZYMES_PHOS_SITE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The ptsH, ptsI, and crr genes of the Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system: a complex operon with several modes of transcription."
    de Reuse H., Danchin A.
    J. Bacteriol. 170:3827-3837(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Sugar transport by the bacterial phosphotransferase system. Molecular cloning and structural analysis of the Escherichia coli ptsH, ptsI, and crr genes."
    Saffen D.W., Presper K.A., Doering T.L., Roseman S.
    J. Biol. Chem. 262:16241-16253(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
    Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
    , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
    DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "Analysis of the ptsH-ptsI-crr region in Escherichia coli K-12: nucleotide sequence of the ptsH gene."
    de Reuse H., Roy A., Danchin A.
    Gene 35:199-207(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-56.
  7. "DNA sequences of the cysK regions of Salmonella typhimurium and Escherichia coli and linkage of the cysK regions to ptsH."
    Byrne C.R., Monroe R.S., Ward K.A., Kredich N.M.
    J. Bacteriol. 170:3150-3157(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-54.
    Strain: K12.
  8. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-11.
    Strain: K12 / EMG2.
  9. "Novel proteins of the phosphotransferase system encoded within the rpoN operon of Escherichia coli. Enzyme IIANtr affects growth on organic nitrogen and the conditional lethality of an erats mutant."
    Powell B.S., Court D.L., Inada T., Nakamura Y., Michotey V., Cui X., Reizer A., Saier M.H. Jr., Reizer J.
    J. Biol. Chem. 270:4822-4839(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PURIFICATION, FUNCTION IN NITROGEN-METABOLIC PTS.
  10. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  11. "The first step in sugar transport: crystal structure of the amino terminal domain of enzyme I of the E. coli PEP: sugar phosphotransferase system and a model of the phosphotransfer complex with HPr."
    Liao D.-I., Silverton E., Seok Y.-J., Lee B.R., Peterkofsky A., Davies D.R.
    Structure 4:861-872(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-259.
  12. "Solution structure of the 30 kDa N-terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system by multidimensional NMR."
    Garrett D.S., Seok Y.-J., Liao D.-I., Peterkofsky A., Gronenborn A.M., Clore G.M.
    Biochemistry 36:2517-2530(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-259.
  13. "Tautomeric state and pKa of the phosphorylated active site histidine in the N-terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system."
    Garrett D.S., Seok Y.-J., Peterkofsky A., Clore G.M., Gronenborn A.M.
    Protein Sci. 7:789-793(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-259.
  14. "Solution structure of the 40,000 Mr phosphoryl transfer complex between the N-terminal domain of enzyme I and HPr."
    Garrett D.S., Seok Y.-J., Peterkofsky A., Gronenborn A.M., Clore G.M.
    Nat. Struct. Biol. 6:166-173(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-259.
  15. "Structure of phosphorylated enzyme I, the phosphoenolpyruvate:sugar phosphotransferase system sugar translocation signal protein."
    Teplyakov A., Lim K., Zhu P.-P., Kapadia G., Chen C.C.H., Schwartz J., Howard A., Reddy P.T., Peterkofsky A., Herzberg O.
    Proc. Natl. Acad. Sci. U.S.A. 103:16218-16223(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, SUBUNIT, SUBSTRATE BINDING AT ARG-332; ASN-454 AND ASP-455, METAL BINDING AT GLU-431 AND ASP-455, ACTIVE SITE HIS-189 AND CYS-502.

Entry informationi

Entry nameiPT1_ECOLI
AccessioniPrimary (citable) accession number: P08839
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: March 16, 2016
This is version 170 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.
Enzyme I of the sugar PTS has been shown in PubMed:7876255 to phosphorylate NPr of the nitrogen-metabolic PTS, though much less efficiently than it does HPr. This process may link carbon and nitrogen assimilation.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.