Reviewed, UniProtKB/Swiss-Prot Q83QP3 (PTFAX_SHIFL)

Names and origin

Protein names

Recommended name:
    Multiphosphoryl transfer protein
      Short name=MTP
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
              EC=2.7.1.-
        Alternative name(s):
            PTS system fructose-like EIIA component

Gene names

Name:	fryA
Ordered Locus Names:	SF2449, S2588

Organism

Shigella flexneri [Complete proteome] [HAMAP]

Taxonomic identifier

623 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Shigella

Protein attributes

Sequence length	831 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

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 By similarity.
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-N(PI)-phosphohistidine-sugar phosphotransferase activity Inferred from electronic annotation. Source: InterPro sugar:hydrogen symporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 831	831	Multiphosphoryl transfer protein		PRO_0000147100
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
Experimental info
	Sequence conflict	381	1	V → A in AAP17769. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q83QP3-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: C2D1C8037293334C	FASTA	831	92,173
	10 20 30 40 50 60 MLTIQFLCPL PNGLHARPAW ELKEQCSQWQ SEITFINHRQ NAKADAKSSL ALIGTGTLFN 70 80 90 100 110 120 DSCSLNISGS DEEQARRVLE EYILVRFIDS 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 PELKPRNNLV LEKPTILVAE DLTPSQFLSL DLKNLAGMIL EKTGRTSHTL 310 320 330 340 350 360 ILARASAIPV LSGLPLDAIA RYAGQPAVLD AQCGVLAINP NDAVSGYYQV AQTLADKRQK 370 380 390 400 410 420 QQAQAAAQLA YSRDNKRIDI VANIGTALEA 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 ARLAKPVDWQ SEMGEVELVI 790 800 810 820 830 MLTLGANEGM NHVKVFSQLA RKLVNKNFRQ SLFAAQDAQS ILTLLETELT F

References

[1]

"Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157." Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y. , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J. Nucleic Acids Res. 30:4432-4441(2002) [PubMed: 12384590] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 301 / Serotype 2a.

[2]

"Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T." Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R. Infect. Immun. 71:2775-2786(2003) [PubMed: 12704152] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700930 / 2457T / Serotype 2a.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE005674 Genomic DNA. Translation: AAN43958.1. AE014073 Genomic DNA. Translation: AAP17769.1.
RefSeq	NP_708251.1. NP_837959.1.
3D structure databases
SMR	Q83QP3. Positions 1-83, 369-679, 684-825.
ModBase	Search...
Genome annotation databases
GeneID	1025242. 1078863.
GenomeReviews	Gene locus SF2449 in contig AE005674_GR. Gene locus S2588 in contig AE014073_GR.
KEGG	sfl:SF2449. sfx:S2588.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG456539.
OMA	IDWQSEM.
Enzyme and pathway databases
BioCyc	SFLE198214:AAN43958.1-MONOMER.
BRENDA	2.7.3.9. 189495.
Family and domain databases
InterPro	IPR008279. PEP-utiliz_enz_mobile_dom. IPR006318. PEP_P_trans. IPR000121. PEP_utilisers. IPR016152. PTrfase/Anion_transptr. IPR002178. PTS_EIIA_2. IPR005698. PTS_HPr_prot. IPR000032. PTS_HPr_prot-like. 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.
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

PTFAX_SHIFL

Accession

Primary (citable) accession number: Q83QP3

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 15, 2003
Last sequence update:	June 1, 2003
Last modified:	February 9, 2010
This is version 58 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)