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Protein

Multiphosphoryl transfer protein 1

Gene

fryA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Multifunctional protein that includes general (non sugar-specific) and sugar-specific components 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). HPr transfers the phosphoryl group to the phosphoryl carrier EIIA, which then transfers it to EIIB (By similarity).By similarity

Catalytic activityi

Phosphoenolpyruvate + protein L-histidine = pyruvate + protein N(pi)-phospho-L-histidine.
Protein EIIA N(pi)-phospho-L-histidine + protein EIIB = protein EIIA + protein EIIB N(pi)-phospho-L-histidine/cysteine.PROSITE-ProRule annotation

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei15 – 151Pros-phosphohistidine intermediate; for HPr activityPROSITE-ProRule annotation
Active sitei298 – 2981Tele-phosphohistidine intermediate; for PTS EI activityPROSITE-ProRule annotation
Binding sitei405 – 4051SubstrateBy similarity
Binding sitei441 – 4411SubstrateBy similarity
Metal bindingi540 – 5401MagnesiumBy similarity
Binding sitei540 – 5401SubstrateBy similarity
Binding sitei561 – 5611Substrate; via carbonyl oxygenBy similarity
Binding sitei562 – 5621Substrate; via amide nitrogenBy similarity
Binding sitei563 – 5631SubstrateBy similarity
Metal bindingi564 – 5641MagnesiumBy similarity
Binding sitei564 – 5641Substrate; via amide nitrogenBy similarity
Active sitei611 – 6111Proton donor; for EI activityBy similarity
Active sitei747 – 7471Tele-phosphohistidine intermediate; for PTS EIIA activityPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

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:G7246-MONOMER.
ECOL316407:JW2380-MONOMER.

Protein family/group databases

TCDBi4.A.2.1.11. the pts fructose-mannitol (fru) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Multiphosphoryl transfer protein 1
Short name:
MTP 1
Including the following 3 domains:
Phosphoenolpyruvate-protein phosphotransferase (EC:2.7.3.9)
Alternative name(s):
Phosphotransferase system enzyme I
Phosphocarrier protein HPr
Short name:
Protein H
Fructose-like phosphotransferase enzyme IIA component 2 (EC:2.7.1.-)
Alternative name(s):
PTS system fructose-like EIIA component 2
Gene namesi
Name:fryA
Synonyms:ypdD
Ordered Locus Names:b2383, JW2380
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG14151. fryA.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 831831Multiphosphoryl transfer protein 1PRO_0000147097Add
BLAST

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP77439.
PRIDEiP77439.

Interactioni

Protein-protein interaction databases

BioGridi4261077. 13 interactions.
DIPiDIP-12817N.
IntActiP77439. 1 interaction.
STRINGi511145.b2383.

Structurei

3D structure databases

ProteinModelPortaliP77439.
SMRiP77439. Positions 116-681, 686-825.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 9090HPrPROSITE-ProRule annotationAdd
BLAST
Domaini685 – 828144PTS EIIA type-2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni266 – 613348PTS EIAdd
BLAST

Domaini

The EIIA domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the EIIB domain.
The Enzyme I (EI) 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

Sequence similaritiesi

Belongs to the PEP-utilizing enzyme family.Curated
Contains 1 HPr domain.PROSITE-ProRule annotation
Contains 1 PTS EIIA type-2 domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105BZ3. Bacteria.
COG1080. LUCA.
COG1925. LUCA.
HOGENOMiHOG000122933.
InParanoidiP77439.
KOiK08483.
K11189.
K11201.
OMAiINHVKVF.
OrthoDBiEOG657JBQ.
PhylomeDBiP77439.

Family and domain databases

Gene3Di1.10.274.10. 1 hit.
3.20.20.60. 1 hit.
3.30.1340.10. 1 hit.
3.40.930.10. 1 hit.
3.50.30.10. 1 hit.
InterProiIPR000032. HPr-like.
IPR008279. PEP-util_enz_mobile_dom.
IPR000121. PEP_util_C.
IPR023151. PEP_util_CS.
IPR016152. PTrfase/Anion_transptr.
IPR006318. PTS_EI-like.
IPR002178. PTS_EIIA_type-2_dom.
IPR008731. PTS_EIN.
IPR004715. PTS_IIA_fruc.
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.
PF00381. PTS-HPr. 1 hit.
PF00359. PTS_EIIA_2. 1 hit.
[Graphical view]
SUPFAMiSSF47831. SSF47831. 1 hit.
SSF51621. SSF51621. 1 hit.
SSF52009. SSF52009. 1 hit.
SSF55594. SSF55594. 1 hit.
SSF55804. SSF55804. 1 hit.
TIGRFAMsiTIGR00848. fruA. 1 hit.
TIGR01417. PTS_I_fam. 1 hit.
PROSITEiPS00742. PEP_ENZYMES_2. 1 hit.
PS51094. PTS_EIIA_TYPE_2. 1 hit.
PS51350. PTS_HPR_DOM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P77439-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLTIQFLCPL PNGLHARPAW ELKEQCSQWQ SEITFINHRQ NAKADAKSSL
60 70 80 90 100
ALIGTGTLFN DSCSLNISGS DEEQARRVLE EYIQVRFIDS DSVQPTQAEL
110 120 130 140 150
TAHPLPRSLS RLNPDLLYGN VLASGVGVGT LTLLQSDSLD SYRAIPASAQ
160 170 180 190 200
DSTRLEHSLA TLAEQLNQQL RERDGESKTI LSAHLSLIQD DEFAGNIRRL
210 220 230 240 250
MTEQHQGLGA AIISNMEQVC AKLSASASDY LRERVSDIRD ISEQLLHITW
260 270 280 290 300
PELKPRNKLV LEKPTILVAE DLTPSQFLSL DLKNLAGMIL EKTGRTSHTL
310 320 330 340 350
ILARASAIPV LSGLPLDAIA RYAGQPAVLD AQCGVLAINP NDAVSGYYQV
360 370 380 390 400
AQTLADKRQK QQAQAAAQLA YSRDNKRIDI AANIGTALEA PGAFANGAEG
410 420 430 440 450
VGLFRTEMLY MDRDSAPDEQ EQFEAYQQVL LAAGDKPIIF RTMDIGGDKS
460 470 480 490 500
IPYLNIPQEE NPFLGYRAVR IYPEFAGLFR TQLRAILRAA SFGNAQLMIP
510 520 530 540 550
MVHSLDQILW VKGEIQKAIV ELKRDGLRHA ETITLGIMVE VPSVCYIIDH
560 570 580 590 600
FCDEVDFFSI GSNDMTQYLY AVDRNNPRVS PLYNPITPSF LRMLQQIVTT
610 620 630 640 650
AHQRGKWVGI CGELGGESRY LPLLLGLGLD ELSMSSPRIP AVKSQLRQLD
660 670 680 690 700
SEACRELARQ ACECRSAQEI EALLTAFTPE EDVRPLLALE NIFVDQDFSN
710 720 730 740 750
KEQAIQFLCG NLGVNGRTEH PFELEEDVWQ REEIVTTGVG FGVAIPHTKS
760 770 780 790 800
QWIRHSSISI ARLAKPIGWQ SEMGEVELVI MLTLGANEGM NHVKVFSQLA
810 820 830
RKLVNKNFRQ SLFAAQDAQS ILTLLETELT F
Length:831
Mass (Da):92,130
Last modified:February 1, 1997 - v1
Checksum:iB9F3E3B6D4EAB597
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC75442.1.
AP009048 Genomic DNA. Translation: BAA16253.1.
PIRiD65012.
RefSeqiNP_416884.1. NC_000913.3.
WP_000955906.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75442; AAC75442; b2383.
BAA16253; BAA16253; BAA16253.
GeneIDi946852.
KEGGiecj:JW2380.
eco:b2383.
PATRICi32120145. VBIEscCol129921_2481.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC75442.1.
AP009048 Genomic DNA. Translation: BAA16253.1.
PIRiD65012.
RefSeqiNP_416884.1. NC_000913.3.
WP_000955906.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP77439.
SMRiP77439. Positions 116-681, 686-825.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261077. 13 interactions.
DIPiDIP-12817N.
IntActiP77439. 1 interaction.
STRINGi511145.b2383.

Protein family/group databases

TCDBi4.A.2.1.11. the pts fructose-mannitol (fru) family.

Proteomic databases

PaxDbiP77439.
PRIDEiP77439.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75442; AAC75442; b2383.
BAA16253; BAA16253; BAA16253.
GeneIDi946852.
KEGGiecj:JW2380.
eco:b2383.
PATRICi32120145. VBIEscCol129921_2481.

Organism-specific databases

EchoBASEiEB3903.
EcoGeneiEG14151. fryA.

Phylogenomic databases

eggNOGiENOG4105BZ3. Bacteria.
COG1080. LUCA.
COG1925. LUCA.
HOGENOMiHOG000122933.
InParanoidiP77439.
KOiK08483.
K11189.
K11201.
OMAiINHVKVF.
OrthoDBiEOG657JBQ.
PhylomeDBiP77439.

Enzyme and pathway databases

BioCyciEcoCyc:G7246-MONOMER.
ECOL316407:JW2380-MONOMER.

Miscellaneous databases

PROiP77439.

Family and domain databases

Gene3Di1.10.274.10. 1 hit.
3.20.20.60. 1 hit.
3.30.1340.10. 1 hit.
3.40.930.10. 1 hit.
3.50.30.10. 1 hit.
InterProiIPR000032. HPr-like.
IPR008279. PEP-util_enz_mobile_dom.
IPR000121. PEP_util_C.
IPR023151. PEP_util_CS.
IPR016152. PTrfase/Anion_transptr.
IPR006318. PTS_EI-like.
IPR002178. PTS_EIIA_type-2_dom.
IPR008731. PTS_EIN.
IPR004715. PTS_IIA_fruc.
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.
PF00381. PTS-HPr. 1 hit.
PF00359. PTS_EIIA_2. 1 hit.
[Graphical view]
SUPFAMiSSF47831. SSF47831. 1 hit.
SSF51621. SSF51621. 1 hit.
SSF52009. SSF52009. 1 hit.
SSF55594. SSF55594. 1 hit.
SSF55804. SSF55804. 1 hit.
TIGRFAMsiTIGR00848. fruA. 1 hit.
TIGR01417. PTS_I_fam. 1 hit.
PROSITEiPS00742. PEP_ENZYMES_2. 1 hit.
PS51094. PTS_EIIA_TYPE_2. 1 hit.
PS51350. PTS_HPR_DOM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "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.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "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.

Entry informationi

Entry nameiPTFX1_ECOLI
AccessioniPrimary (citable) accession number: P77439
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: February 1, 1997
Last modified: July 6, 2016
This is version 150 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The Enzyme I (EI) 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).By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. 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.