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Protein

Multiphosphoryl transfer protein

Gene

fryA

Organism
Escherichia coli O157:H7
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

Mg2+By similarity

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

BioCyciECOL386585:GJFA-3217-MONOMER.
ECOO157:Z3648-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Multiphosphoryl transfer protein
Short name:
MTP
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 (EC:2.7.1.-)
Alternative name(s):
PTS system fructose-like EIIA component
Gene namesi
Name:fryA
Ordered Locus Names:Z3648, ECs3263
OrganismiEscherichia coli O157:H7
Taxonomic identifieri83334 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000558 Componenti: Chromosome
  • UP000002519 Componenti: Chromosome

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 proteinPRO_0000147099Add
BLAST

Keywords - PTMi

Phosphoprotein

Interactioni

Protein-protein interaction databases

STRINGi155864.Z3648.

Structurei

3D structure databases

ProteinModelPortaliQ8XBQ8.
SMRiQ8XBQ8. Positions 1-85, 116-680, 683-825.
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.
COG1762. LUCA.
COG1925. LUCA.
HOGENOMiHOG000122933.
KOiK08483.
K11189.
K11201.
OMAiINHVKVF.
OrthoDBiEOG657JBQ.

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.

Q8XBQ8-1 [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 AIIRNMEQVC AKLSASASDY LRERVSDIRD ISEQLLHITW
260 270 280 290 300
PELKPRNNLV 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 MDRDSEPDEQ EQFEAYQQVL LAAGDKPIIF RTMDIGGDKS
460 470 480 490 500
IPYLNIPQEE NPFLGYRAVR IYPEFAGLFR TQLRAILRAA SFGNAQLMIP
510 520 530 540 550
MVHGLDQILW 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 NIFVDQAFSN
710 720 730 740 750
KEQAIQFLCG NLGVNGRTEH PFELEEDVWQ REEIVTTGVG FGVAIPHTKS
760 770 780 790 800
QWIRHSSISI ARLAKPVDWQ SEMGEVELVI MLTLGANEGM NHVKVFSQLA
810 820 830
RKLVNKNFRQ SLFAAQDAQS ILTLLETELT F
Length:831
Mass (Da):92,213
Last modified:March 1, 2002 - v1
Checksum:iA6E746EB07BBBC0A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005174 Genomic DNA. Translation: AAG57509.1.
BA000007 Genomic DNA. Translation: BAB36686.1.
PIRiA85881.
G91036.
RefSeqiNP_311290.1. NC_002695.1.
WP_000955897.1. NZ_LPWC01000609.1.

Genome annotation databases

EnsemblBacteriaiAAG57509; AAG57509; Z3648.
BAB36686; BAB36686; BAB36686.
GeneIDi915635.
KEGGiece:Z3648.
ecs:ECs3263.
PATRICi18355926. VBIEscCol44059_3163.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005174 Genomic DNA. Translation: AAG57509.1.
BA000007 Genomic DNA. Translation: BAB36686.1.
PIRiA85881.
G91036.
RefSeqiNP_311290.1. NC_002695.1.
WP_000955897.1. NZ_LPWC01000609.1.

3D structure databases

ProteinModelPortaliQ8XBQ8.
SMRiQ8XBQ8. Positions 1-85, 116-680, 683-825.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi155864.Z3648.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG57509; AAG57509; Z3648.
BAB36686; BAB36686; BAB36686.
GeneIDi915635.
KEGGiece:Z3648.
ecs:ECs3263.
PATRICi18355926. VBIEscCol44059_3163.

Phylogenomic databases

eggNOGiENOG4105BZ3. Bacteria.
COG1080. LUCA.
COG1762. LUCA.
COG1925. LUCA.
HOGENOMiHOG000122933.
KOiK08483.
K11189.
K11201.
OMAiINHVKVF.
OrthoDBiEOG657JBQ.

Enzyme and pathway databases

BioCyciECOL386585:GJFA-3217-MONOMER.
ECOO157:Z3648-MONOMER.

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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
  2. "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
    Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.
    , Kuhara S., Shiba T., Hattori M., Shinagawa H.
    DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Entry informationi

Entry nameiPTFAX_ECO57
AccessioniPrimary (citable) accession number: Q8XBQ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: March 1, 2002
Last modified: July 6, 2016
This is version 101 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

Documents

  1. 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.