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PR00107

Identifier
PHOSPHOCPHPR  [View Relations]  [View Alignment]  
Accession
PR00107
No. of Motifs
3
Creation Date
08-MAR-1995  (UPDATE 07-JUN-1999)
Title
Phosphocarrier protein signature
Database References

PROSITE; PS00369 PTS_HPR_HIS; PS00589 PTS_HPR_SER
BLOCKS; BL00369
PFAM; PF00381 PTS-HPr
INTERPRO; IPR001020
PDB; 1HID
SCOP; 1HID
CATH; 1HID
Literature References
1. VAN NULAND, N.A.M., BOELENS, R., SCHEEK, R.M. AND ROBILLARD, G.T.
High-resolution structure of the phosphorylated form of the histidine-
containing phosphocarrier protein HPr from Escherichia coli determined
by restrained molecular dynamics from NRM-NOE data.
J.MOL.BIOL. 246 180-193 (1995).
 
2. LIAO, D-I. AND HERZBERG, O.
Refined structures of the active Ser83-Cys and impaired Ser46-Asp
histidine-containing phosphocarrier proteins.
STRUCTURE 2 1203-1216 (1994).

Documentation
The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS)
is a major carbohydrate transport system in bacteria. The PTS catalyses
the phosphorylation of sugar substrates during their translocation across
the cell membrane. The mechanism involves the transfer of a phosphoryl
group from phosphoenolpyruvate (PEP) via enzyme I (EI) to enzyme II (EII)
of the PTS system, which in turn transfers it to a phosphocarrier protein
(HPr) [1,2].
 
HPr is a small (79-90 amino acid) cytoplasmic protein - in certain 
bacteria, HPr is a domain in a larger protein that includes an EIII(Fru)
(IIA) domain, and in some cases also the EI domain. A conserved N-terminal
His serves as an acceptor for the phosphoryl group of EI, and a centrally
located conserved Ser (in Gram-positive bacteria only) is phosphorylated
by an ATP-dependent protein kinase, which process may play a role in
sugar transport. The phosphorylation sites are well conserved.
 
The structure of HPr comprises a 4-stranded anti-parallel beta-sheet, with
3 alpha-helices that pack against one face of the sheet, a fold known as an
open-face beta-sandwich [2]. The topology can be described as that of a
right-handed alpha-/beta-jelly-roll, by analogy with the beta-sandwich
jelly-roll fold of viral coat proteins, legume lectins, and so on. The
catalytic His and the regulatory Ser are located on the surface of the
protein, such that they can be phosphorylated without invoking
conformational changes.  
 
PHOSPHOCPHPR is a 3-element fingerprint that provides a signature for HPr
phosphocarrier proteins. The fingerprint was derived from an initial
alignment of 6 sequences: the motifs were drawn from short conserved
regions spanning the full alignment length, motifs 1 and 2 including the
His and Ser phosphorylation sites encoded by PROSITE patterns PTS_HPR_HIS
(PS00369) and PTS_HPR_SER (PS00589). Two iterations on OWL25.2 were
required to reach convergence, at which point a true set comprising 21
sequences was identified.
 
An update on SPTR37_9f identified a true set of 26 sequences.
Summary Information
26 codes involving  3 elements
0 codes involving 2 elements
Composite Feature Index
3262626
2000
123
True Positives
O06976        O51507        O69250        P94759        
PTF1_RHOCA PTF1_XANCP PTFA_ECOLI PTFA_HAEIN
PTFA_SALTY PTHP_ALCEU PTHP_BACST PTHP_BACSU
PTHP_ECOLI PTHP_ENTFA PTHP_HAEIN PTHP_KLEPN
PTHP_LACSK PTHP_LISMO PTHP_MYCCA PTHP_MYCGE
PTHP_MYCPN PTHP_STAAU PTHP_STACA PTHP_STRMU
PTHP_STRSL PTHP_TREPA
Sequence Titles
O06976      HYPOTHETICAL 9.3 KD PROTEIN - BACILLUS SUBTILIS. 
O51507 PHOSPHOCARRIER PROTEIN HPR (PTSH-2) - BORRELIA BURGDORFERI (LYME DISEASE SPIROCHETE).
O69250 HPR PROTEIN - BACILLUS MEGATERIUM.
P94759 PTS SYSTEM, FRUCTOSE-SPECIFIC IIA/FPR COMPONENT (EIIA-FRU) (FRUCTOSE-PERMEASE IIA/FPR COMPONENT) (PHOSPHOTRANSFERASE ENZYME II, A/FPR COMPONENT) (EC 2.7.1.69) (PHOSPHOTRANSFERASE FPR PROTEIN) (PSEUDO-HPR) (EIII-FRU) - ESCHERICHIA COLI.
PTF1_RHOCA Multiphosphoryl transfer protein (MTP) [Includes: Phosphoenolpyruvate- protein phosphotransferase (EC 2.7.3.9) (Phosphotransferase system, enzyme I); Phosphocarrier protein HPR (Protein H); PTS system, fructose-specific IIA component (EIIA-FRU) (Fructose-permease IIA component) (Phosphotransferase enzyme II, A component) (EC 2.7.1.69) (EIII-FRU)] - Rhodobacter capsulatus (Rhodopseudomonas capsulata).
PTF1_XANCP Multiphosphoryl transfer protein (MTP) [Includes: Phosphoenolpyruvate- protein phosphotransferase (EC 2.7.3.9) (Phosphotransferase system, enzyme I); Phosphocarrier protein HPR (Protein H); PTS system, fructose-specific IIA component (EIIA-FRU) (Fructose-permease IIA component) (Phosphotransferase enzyme II, A component) (EC 2.7.1.69) (EIII-FRU)] - Xanthomonas campestris (pv. campestris).
PTFA_ECOLI PTS SYSTEM, FRUCTOSE-SPECIFIC IIA/FPR COMPONENT (EIIA-FRU) (FRUCTOSE- PERMEASE IIA/FPR COMPONENT) (PHOSPHOTRANSFERASE ENZYME II, A/FPR COMPONENT) (EC 2.7.1.69) (PHOSPHOTRANSFERASE FPR PROTEIN) (PSEUDO- HPR) (EIII-FRU) (FRUCTOSE PTS DIPHOSPHORYL TRANSFER PROTEIN) - ESCHERICHIA COLI.
PTFA_HAEIN PTS SYSTEM, FRUCTOSE-SPECIFIC IIA/FPR COMPONENT (EIIA-FRU) (FRUCTOSE- PERMEASE IIA/HPR COMPONENT) (PHOSPHOTRANSFERASE ENZYME II, A/HPR COMPONENT) (EC 2.7.1.69) (PHOSPHOTRANSFERASE FPR PROTEIN) (PSEUDO- HPR) (EIII-FRU) (FRUCTOSE PTS DIPHOSPHORYL TRANSFER PROTEIN) - HAEMOPHILUS INFLUENZAE.
PTFA_SALTY PTS SYSTEM, FRUCTOSE-SPECIFIC IIA/FPR COMPONENT (EIIA-FRU) (FRUCTOSE- PERMEASE IIA/HPR COMPONENT) (PHOSPHOTRANSFERASE ENZYME II, A/HPR COMPONENT) (EC 2.7.1.69) (PHOSPHOTRANSFERASE FPR PROTEIN) (PSEUDO- HPR) (EIII-FRU) (FRUCTOSE PTS DIPHOSPHORYL TRANSFER PROTEIN) - SALMONELLA TYPHIMURIUM.
PTHP_ALCEU PHOSPHOCARRIER PROTEIN HPR (HISTIDINE-CONTAINING PROTEIN) (PROTEIN H) - ALCALIGENES EUTROPHUS.
PTHP_BACST PHOSPHOCARRIER PROTEIN HPR (HISTIDINE-CONTAINING PROTEIN) - BACILLUS STEAROTHERMOPHILUS.
PTHP_BACSU PHOSPHOCARRIER PROTEIN HPR (HISTIDINE-CONTAINING PROTEIN) - BACILLUS SUBTILIS.
PTHP_ECOLI PHOSPHOCARRIER PROTEIN HPR (HISTIDINE-CONTAINING PROTEIN) - ESCHERICHIA COLI, AND SALMONELLA TYPHIMURIUM.
PTHP_ENTFA PHOSPHOCARRIER PROTEIN HPR (HISTIDINE-CONTAINING PROTEIN) - ENTEROCOCCUS FAECALIS (STREPTOCOCCUS FAECALIS).
PTHP_HAEIN PHOSPHOCARRIER PROTEIN HPR (HISTIDINE-CONTAINING PROTEIN) - HAEMOPHILUS INFLUENZAE.
PTHP_KLEPN PHOSPHOCARRIER PROTEIN HPR (HISTIDINE-CONTAINING PROTEIN) - KLEBSIELLA PNEUMONIAE.
PTHP_LACSK PHOSPHOCARRIER PROTEIN HPR (HISTIDINE-CONTAINING PROTEIN) - LACTOBACILLUS SAKE.
PTHP_LISMO PHOSPHOCARRIER PROTEIN HPR (HISTIDINE-CONTAINING PROTEIN) - LISTERIA MONOCYTOGENES.
PTHP_MYCCA PHOSPHOCARRIER PROTEIN HPR (HISTIDINE-CONTAINING PROTEIN) - MYCOPLASMA CAPRICOLUM.
PTHP_MYCGE PHOSPHOCARRIER PROTEIN HPR (HISTIDINE-CONTAINING PROTEIN) - MYCOPLASMA GENITALIUM.
PTHP_MYCPN PHOSPHOCARRIER PROTEIN HPR (HISTIDINE-CONTAINING PROTEIN) - MYCOPLASMA PNEUMONIAE.
PTHP_STAAU PHOSPHOCARRIER PROTEIN HPR (HISTIDINE-CONTAINING PROTEIN) - STAPHYLOCOCCUS AUREUS.
PTHP_STACA PHOSPHOCARRIER PROTEIN HPR (HISTIDINE-CONTAINING PROTEIN) - STAPHYLOCOCCUS CARNOSUS.
PTHP_STRMU PHOSPHOCARRIER PROTEIN HPR (HISTIDINE-CONTAINING PROTEIN) - STREPTOCOCCUS MUTANS.
PTHP_STRSL PHOSPHOCARRIER PROTEIN HPR (HISTIDINE-CONTAINING PROTEIN) - STREPTOCOCCUS SALIVARIUS.
PTHP_TREPA PHOSPHOCARRIER PROTEIN HPR (HISTIDINE-CONTAINING PROTEIN) - TREPONEMA PALLIDUM.
Scan History
OWL25_2    2  100  NSINGLE    
SPTR37_9f 2 47 NSINGLE
Initial Motifs
Motif 1  width=17
Element Seqn Id St Int Rpt
GIHARPATMLVQTASKF PTHP_STACA 13 13 -
GIHARPATLLVQTASKF PTHP_ENTFA 13 13 -
GLHARPGTMLVNTIKQF PTFA_SALTY 297 297 -
GLHTRPAAQFVKEAKGF PTHP_KLEPN 13 13 -
GLHARPATTLVDLAKGF PTF1_RHOCA 169 169 -
GLHARASAKLTQLAGNF PTHP_ALCEU 13 13 -

Motif 2 width=16
Element Seqn Id St Int Rpt
NGKKVNLKSIMGVMSL PTHP_STACA 38 8 -
KGKSVNLKSIMGVMSL PTHP_ENTFA 38 8 -
TGKPANGRSLMKVVAL PTFA_SALTY 325 11 -
NGKSASAKSLFKLQTL PTHP_KLEPN 38 8 -
GAKVANGKSLISLLNL PTF1_RHOCA 194 8 -
NGRQVDAKSIMGVMML PTHP_ALCEU 38 8 -

Motif 3 width=18
Element Seqn Id St Int Rpt
LGVGKDAEITIYADGSDE PTHP_STACA 53 -1 -
LGVGQGSDVTITVDGADE PTHP_ENTFA 53 -1 -
LGVKKGHRLRFTAQGEDA PTFA_SALTY 340 -1 -
LGLTQGTVVTLSAEGEDE PTHP_KLEPN 53 -1 -
LGAAQGAALRISAEGADA PTF1_RHOCA 209 -1 -
LAAGIGSTVTLETDGPDE PTHP_ALCEU 53 -1 -
Final Motifs
Motif 1  width=17
Element Seqn Id St Int Rpt
GIHARPATLLVQTASKF PTHP_LACSK 13 13 -
GIHARPATLLVQTASKF PTHP_STRSL 13 13 -
GIHARPATLLVQTASKF PTHP_STRMU 13 13 -
GIHARPATMLVQTASKF PTHP_STAAU 13 13 -
GIHARPATMLVQTASKF PTHP_STACA 13 13 -
GIHARPATTLVQAASKF O69250 13 13 -
GIHARPATLLVQTASKF PTHP_ENTFA 13 13 -
GIHARPATVLVQTASKY PTHP_BACSU 12 12 -
GIHARPATILVQTASKF PTHP_BACST 13 13 -
GIHARPATLLVQAASKY PTHP_LISMO 13 13 -
GLQARPAALFVQEANRF O06976 13 13 -
GLHTRPAAQFVKEAKGF PTHP_ECOLI 13 13 -
GLHARPGTMLVNTIKQF P94759 297 297 -
GLHARPGTMLVNTIKQF PTFA_ECOLI 297 297 -
GLHARPGTMLVNTIKQF PTFA_SALTY 297 297 -
GLHTRPAAQFVKEAKGF PTHP_KLEPN 13 13 -
GLHARPATTLVDLAKGF PTF1_RHOCA 169 169 -
GLHTRPAAQFVKEAKAF PTHP_HAEIN 13 13 -
GLHARPASVLAKEASKF PTHP_MYCCA 12 12 -
GLHARASAKLTQLAGNF PTHP_ALCEU 13 13 -
GLHARPATRWAETARGF PTF1_XANCP 173 173 -
GIHARPASILASEASKF PTHP_MYCGE 13 13 -
GIHARPASIIAGEANKF PTHP_MYCPN 13 13 -
GVHARPAALIVQAASRF PTHP_TREPA 13 13 -
GLHARPSANLVNEVKKF PTFA_HAEIN 298 298 -
GLHVRPASTFVKKAKEY O51507 13 13 -

Motif 2 width=16
Element Seqn Id St Int Rpt
KGKSVNLKSIMGVMSL PTHP_LACSK 38 8 -
KGKAVNLKSIMGVMSL PTHP_STRSL 38 8 -
KGKAVNLKSIMGVMSL PTHP_STRMU 38 8 -
NGKKVNLKSIMGVMSL PTHP_STAAU 38 8 -
NGKKVNLKSIMGVMSL PTHP_STACA 38 8 -
NGKTVNLKSIMGVMSL O69250 38 8 -
KGKSVNLKSIMGVMSL PTHP_ENTFA 38 8 -
NGKTVNLKSIMGVMSL PTHP_BACSU 37 8 -
NGKTVNLKSIMGVMSL PTHP_BACST 38 8 -
TGKKVNLKSIMGVMSL PTHP_LISMO 38 8 -
DGKKVNAKSIMGLMSL O06976 38 8 -
NGKSASAKSLFKLQTL PTHP_ECOLI 38 8 -
TGKPANGRSLMKVVAL P94759 325 11 -
TGKPANGRSLMKVVAL PTFA_ECOLI 325 11 -
TGKPANGRSLMKVVAL PTFA_SALTY 325 11 -
NGKSASAKSLFKLQTL PTHP_KLEPN 38 8 -
GAKVANGKSLISLLNL PTF1_RHOCA 194 8 -
GGKSASAKSLFKLQTL PTHP_HAEIN 38 8 -
NEKQGNLKSIMNVMAM PTHP_MYCCA 37 8 -
NGRQVDAKSIMGVMML PTHP_ALCEU 38 8 -
GDQAADAKSLVGLLQL PTF1_XANCP 198 8 -
SGVEGNIKSIINLMSL PTHP_MYCGE 39 9 -
SGVEGNIKSIINLMSL PTHP_MYCPN 39 9 -
DTIRVNAKSIMGVMAM PTHP_TREPA 38 8 -
NSQLVSAKSLMKIVAL PTFA_HAEIN 450 135 -
DGKSVSGKSLFRLQTL O51507 38 8 -

Motif 3 width=18
Element Seqn Id St Int Rpt
LGVGQGADVTISAEGADE PTHP_LACSK 53 -1 -
LGVGQGADVTISAEGADA PTHP_STRSL 53 -1 -
LGVGQGADVTITAEGADA PTHP_STRMU 53 -1 -
LGVGKDAEITIYADGSDE PTHP_STAAU 53 -1 -
LGVGKDAEITIYADGSDE PTHP_STACA 53 -1 -
LGIQKGATITISAEGSDE O69250 53 -1 -
LGVGQGSDVTITVDGADE PTHP_ENTFA 53 -1 -
LGIAKGAEITISASGADE PTHP_BACSU 52 -1 -
LGIPKGATIKITAEGADA PTHP_BACST 53 -1 -
LGIGKGADITIYTEGSDE PTHP_LISMO 53 -1 -
LAVSTGTEVTLIAQGEDE O06976 53 -1 -
LGLTQGTVVTISAEGEDE PTHP_ECOLI 53 -1 -
LGVKKGHRLRFTAQGADA P94759 340 -1 -
LGVKKGHRLRFTAQGADA PTFA_ECOLI 340 -1 -
LGVKKGHRLRFTAQGEDA PTFA_SALTY 340 -1 -
LGLTQGTVVTLSAEGEDE PTHP_KLEPN 53 -1 -
LGAAQGAALRISAEGADA PTF1_RHOCA 209 -1 -
LALTQGTILTISADGEDE PTHP_HAEIN 53 -1 -
MAIKTGTEITIQADGNDA PTHP_MYCCA 52 -1 -
LAAGIGSTVTLETDGPDE PTHP_ALCEU 53 -1 -
LGLRAGDSITVSAKGSDA PTF1_XANCP 213 -1 -
LGIRHNDNITIKADGADE PTHP_MYCGE 54 -1 -
LGIKQNDHITIKAEGTDE PTHP_MYCPN 54 -1 -
MAAGCGSELELVVEGPDE PTHP_TREPA 53 -1 -
LGVVKGTRLRFVATGEEA PTFA_HAEIN 465 -1 -
LELSSGKKLLICAEGEDE O51507 53 -1 -