Reviewed, UniProtKB/Swiss-Prot P77439 (PTFX1_ECOLI)

Names and origin

Protein names

Recommended name:
    Multiphosphoryl transfer protein 1
      Short name=MTP 1
Including the following 3 domains:
    1- Recommended name:
            Phosphoenolpyruvate-protein phosphotransferase
              EC=2.7.3.9
        Alternative name(s):
            Phosphotransferase system enzyme I
    2- Recommended name:
            Phosphocarrier protein HPr
                Short name=Protein H
    3- Recommended name:
            Fructose-like phosphotransferase enzyme IIA component 2
              EC=2.7.1.-
        Alternative name(s):
            PTS system fructose-like EIIA component 2

Gene names

Name:	fryA
Synonyms:	ypdD
Ordered Locus Names:	b2383, JW2380

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	831 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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.
Catalytic activity	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.
Cofactor	Magnesium.
Subcellular location	Cytoplasm Probable.
Domain	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.
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.
Sequence similarities	Belongs to the PEP-utilizing enzyme family. Contains 1 HPr domain. Contains 1 PTS EIIA type-2 domain.

Ontologies

Keywords
Biological process	Phosphotransferase system Sugar transport Transport
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	phosphoenolpyruvate-dependent sugar phosphotransferase system Inferred from electronic annotation. Source: UniProtKB-KW phosphorylation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: InterPro
Molecular function	kinase activity Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoenolpyruvate-protein phosphotransferase activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction. Source: IntAct protein-N(PI)-phosphohistidine-sugar phosphotransferase activity Inferred from electronic annotation. Source: InterPro sugar:hydrogen symporter activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
aceE	P0AFG8	1	EBI-545399,EBI-542683

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 831	831	Multiphosphoryl transfer protein 1		PRO_0000147097
Regions
	Domain	1 – 90	90	HPr
	Domain	685 – 828	144	PTS EIIA type-2
	Region	266 – 613	348	PTS EI
Sites
	Active site	15	1	Pros-phosphohistidine intermediate; for HPr activity By similarity
	Active site	298	1	Tele-phosphohistidine intermediate; for PTS EI activity By similarity
	Active site	611	1	Proton donor; for EI activity By similarity
	Active site	747	1	Tele-phosphohistidine intermediate; for PTS EIIA activity By similarity
	Metal binding	540	1	Magnesium By similarity
	Metal binding	564	1	Magnesium By similarity
	Binding site	405	1	Substrate By similarity
	Binding site	441	1	Substrate By similarity
	Binding site	540	1	Substrate By similarity
	Binding site	561	1	Substrate; via carbonyl oxygen By similarity
	Binding site	562	1	Substrate; via amide nitrogen By similarity
	Binding site	563	1	Substrate By similarity
	Binding site	564	1	Substrate; via amide nitrogen By similarity

Sequences

	Sequence		Length	Mass (Da)
	P77439-1 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: B9F3E3B6D4EAB597	FASTA	831	92,130
	10 20 30 40 50 60 MLTIQFLCPL PNGLHARPAW ELKEQCSQWQ SEITFINHRQ NAKADAKSSL ALIGTGTLFN 70 80 90 100 110 120 DSCSLNISGS DEEQARRVLE EYIQVRFIDS DSVQPTQAEL TAHPLPRSLS RLNPDLLYGN 130 140 150 160 170 180 VLASGVGVGT LTLLQSDSLD SYRAIPASAQ DSTRLEHSLA TLAEQLNQQL RERDGESKTI 190 200 210 220 230 240 LSAHLSLIQD DEFAGNIRRL MTEQHQGLGA AIISNMEQVC AKLSASASDY LRERVSDIRD 250 260 270 280 290 300 ISEQLLHITW PELKPRNKLV LEKPTILVAE DLTPSQFLSL DLKNLAGMIL EKTGRTSHTL 310 320 330 340 350 360 ILARASAIPV LSGLPLDAIA RYAGQPAVLD AQCGVLAINP NDAVSGYYQV AQTLADKRQK 370 380 390 400 410 420 QQAQAAAQLA YSRDNKRIDI AANIGTALEA PGAFANGAEG VGLFRTEMLY MDRDSAPDEQ 430 440 450 460 470 480 EQFEAYQQVL LAAGDKPIIF RTMDIGGDKS IPYLNIPQEE NPFLGYRAVR IYPEFAGLFR 490 500 510 520 530 540 TQLRAILRAA SFGNAQLMIP MVHSLDQILW VKGEIQKAIV ELKRDGLRHA ETITLGIMVE 550 560 570 580 590 600 VPSVCYIIDH FCDEVDFFSI GSNDMTQYLY AVDRNNPRVS PLYNPITPSF LRMLQQIVTT 610 620 630 640 650 660 AHQRGKWVGI CGELGGESRY LPLLLGLGLD ELSMSSPRIP AVKSQLRQLD SEACRELARQ 670 680 690 700 710 720 ACECRSAQEI EALLTAFTPE EDVRPLLALE NIFVDQDFSN KEQAIQFLCG NLGVNGRTEH 730 740 750 760 770 780 PFELEEDVWQ REEIVTTGVG FGVAIPHTKS QWIRHSSISI ARLAKPIGWQ SEMGEVELVI 790 800 810 820 830 MLTLGANEGM NHVKVFSQLA RKLVNKNFRQ SLFAAQDAQS ILTLLETELT F

References

[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: 9205837] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] 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: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U00096 Genomic DNA. Translation: AAC75442.1. AP009048 Genomic DNA. Translation: BAA16253.1.
PIR	D65012.
RefSeq	AP_002983.1. NP_416884.1.
3D structure databases
HSSP	HSSP built from PDB template 1EZC based on UniProtKB P08839.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:12817N.
IntAct	P77439. 1 interaction.
Genome annotation databases
GeneID	946852.
GenomeReviews	Gene locus JW2380 in contig AP009048_GR. Gene locus b2383 in contig U00096_GR.
KEGG	ecj:JW2380. eco:b2383.
Organism-specific databases
EchoBASE	EB3903.
EcoGene	EG14151. fryA.
CMR	Search...
Phylogenomic databases
HOGENOM	P77439.
OMA	P77439. IDWQSEM.
Enzyme and pathway databases
BioCyc	EcoCyc:G7246-MON.
Family and domain databases
InterPro	IPR008279. PEP_mobile. IPR018274. PEP_mobile_CS. IPR006318. PEP_P_trans. IPR000121. PEP_utilizers. IPR002178. PTS_EIIA_2. IPR001020. PTS_HPr_HisP_S. IPR005698. PTS_HPr_prot. IPR000032. PTS_HPr_prot-like. IPR002114. PTS_HPr_SerP_S. IPR004715. PTS_IIA_fruc. IPR008731. PTS_PEP_utilis_N. IPR015813. Pyrv/PenolPyrv_Kinase_cat. [Graphical view]
Gene3D	G3DSA:3.50.30.10. PEP_mobile. 1 hit. G3DSA:3.30.1340.10. PTS_HPr_protein. 1 hit. G3DSA:1.10.274.10. PTS_PEP_utilis_N. 1 hit. G3DSA:3.20.20.60. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
Pfam	PF05524. 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]
PRINTS	PR01736. PHPHTRNFRASE.
ProDom	PD002238. HPr_protein. 1 hit. PD000940. PEP_utilizers. 1 hit. PD001689. PTS_EIIA_2. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR00848. fruA. 1 hit. TIGR01417. PTS_I_fam. 1 hit.
PROSITE	PS00742. PEP_ENZYMES_2. 1 hit. PS00370. PEP_ENZYMES_PHOS_SITE. False negative. PS51094. PTS_EIIA_TYPE_2. 1 hit. PS51350. PTS_HPR_DOM. 1 hit. PS00369. PTS_HPR_HIS. False negative. PS00589. PTS_HPR_SER. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PTFX1_ECOLI

Accession

Primary (citable) accession number: P77439

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	February 1, 1997
Last modified:	June 16, 2009
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)