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7  structures 2956  species 0  interactions 15740  sequences 61  architectures

Family: PTS_EIIC (PF02378)

Summary: Phosphotransferase system, EIIC

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This is the Wikipedia entry entitled "Saccharide transporter". More...

Saccharide transporter Edit Wikipedia article

Phosphotransferase system, EIIC
3qnq.png
Crystal structure of a phosphorylation-coupled saccharide transporter. PDB 3qnq.[1]
Identifiers
SymbolPTS_EIIC
PfamPF02378
Pfam clanCL0493
InterProIPR003352
TCDB4.A.3
OPM superfamily226
OPM protein3qnq

The bacterial phosphoenolpyruvate: sugar phosphotransferase system (PTS) is a multi-protein system involved in the regulation of a variety of metabolic and transcriptional processes. The PTS catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane. The general mechanism of the PTS is the following: a phosphoryl group from phosphoenolpyruvate (PEP) is transferred to enzyme-I (EI) of PTS which in turn transfers it to a phosphoryl carrier protein (HPr). Phospho-HPr then transfers the phosphoryl group to a sugar-specific permease which consists of at least three structurally distinct domains (IIA, IIB, and IIC) [2] which can either be fused together in a single polypeptide chain or exist as two or three interactive chains, formerly called enzymes II (EII) and III (EIII). The IIC domain catalyzes the transfer of a phosphoryl group from IIB to the sugar substrate.

References

  1. ^ Cao Y, Jin X, Levin EJ, Huang H, Zong Y, Quick M, Weng J, Pan Y, Love J, Punta M, Rost B, Hendrickson WA, Javitch JA, Rajashankar KR, Zhou M (May 2011). "Crystal structure of a phosphorylation-coupled saccharide transporter". Nature. 473 (7345): 50–4. Bibcode:2011Natur.473...50C. doi:10.1038/nature09939. PMC 3201810. PMID 21471968.
  2. ^ Saier MH, Reizer J (March 1992). "Proposed uniform nomenclature for the proteins and protein domains of the bacterial phosphoenolpyruvate: sugar phosphotransferase system". Journal of Bacteriology. 174 (5): 1433–8. doi:10.1128/jb.174.5.1433-1438.1992. PMC 206537. PMID 1537788.
This article incorporates text from the public domain Pfam and InterPro: IPR003352

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Phosphotransferase system, EIIC Provide feedback

The bacterial phosphoenolpyruvate: sugar phosphotransferase system (PTS) is a multi-protein system involved in the regulation of a variety of metabolic and transcriptional processes. The sugar-specific permease of the PTS consists of three domains (IIA, IIB and IIC). The IIC domain catalyses the transfer of a phosphoryl group from IIB to the sugar substrate.

Literature references

  1. Reizer J, Paulsen IT, Reizer A, Titgemeyer F, Saier MH Jr; , Microb Comp Genomics 1996;1:151-164.: Novel phosphotransferase system genes revealed by bacterial genome analysis: the complete complement of pts genes in mycoplasma genitalium. PUBMED:9689210 EPMC:9689210


Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR003352

The bacterial phosphoenolpyruvate: sugar phosphotransferase system (PTS) is a multi-protein system involved in the regulation of a variety of metabolic and transcriptional processes. The PTS catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane. The general mechanism of the PTS is the following: a phosphoryl group from phosphoenolpyruvate (PEP) is transferred to enzyme-I (EI) of PTS which in turn transfers it to a phosphoryl carrier protein (HPr). Phospho-HPr then transfers the phosphoryl group to a sugar-specific permease which consists of at least three structurally distinct domains (IIA, IIB, and IIC) [ PUBMED:1537788 ] which can either be fused together in a single polypeptide chain or exist as two or three interactive chains, formerly called enzymes II (EII) and III (EIII). The IIC domain catalyzes the transfer of a phosphoryl group from IIB to the sugar substrate.

PTS systems commonly occur in bacteria. An archaeal version has also been discovered [ PUBMED:22493022 ]. This entry identifies both the bacterial family members and archaeal homologues.

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan PTS_EIIC (CL0493), which has the following description:

The clan contains the following 2 members:

PTS_EIIC PTS_EIIC_2

Alignments

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

  Seed
(49)
Full
(15740)
Representative proteomes UniProt
(109110)
RP15
(1160)
RP35
(7225)
RP55
(16053)
RP75
(32417)
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PP/heatmap 1            

1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(49)
Full
(15740)
Representative proteomes UniProt
(109110)
RP15
(1160)
RP35
(7225)
RP55
(16053)
RP75
(32417)
Alignment:
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(49)
Full
(15740)
Representative proteomes UniProt
(109110)
RP15
(1160)
RP35
(7225)
RP55
(16053)
RP75
(32417)
Raw Stockholm Download   Download   Download   Download   Download   Download    
Gzipped Download   Download   Download   Download   Download   Download    

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

Note: You can also download the data file for the tree.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Pfam-B_639 (release 5.2)
Previous IDs: none
Type: Family
Sequence Ontology: SO:0100021
Author: Mian N , Bateman A
Number in seed: 49
Number in full: 15740
Average length of the domain: 297.30 aa
Average identity of full alignment: 19 %
Average coverage of the sequence by the domain: 56.75 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 30.7 30.7
Trusted cut-off 30.7 30.7
Noise cut-off 30.6 30.6
Model length: 324
Family (HMM) version: 21
Download: download the raw HMM for this family

Species distribution

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Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
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Viroids Viroids Unclassified sequence Unclassified sequence

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Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the PTS_EIIC domain has been found. There are 7 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information
C7NB69 View 3D Structure Click here
D4GYE5 View 3D Structure Click here
O05507 View 3D Structure Click here
O31645 View 3D Structure Click here
O34521 View 3D Structure Click here
O65989 View 3D Structure Click here
P00550 View 3D Structure Click here
P05306 View 3D Structure Click here
P08722 View 3D Structure Click here
P09323 View 3D Structure Click here
P12655 View 3D Structure Click here
P15400 View 3D Structure Click here
P17334 View 3D Structure Click here
P19642 View 3D Structure Click here
P20166 View 3D Structure Click here
P20966 View 3D Structure Click here
P24241 View 3D Structure Click here
P31452 View 3D Structure Click here
P32154 View 3D Structure Click here
P36672 View 3D Structure Click here
P37439 View 3D Structure Click here
P39584 View 3D Structure Click here
P39794 View 3D Structure Click here
P39816 View 3D Structure Click here
P40739 View 3D Structure Click here
P42956 View 3D Structure Click here
P46317 View 3D Structure Click here
P47308 View 3D Structure Click here
P47315 View 3D Structure Click here
P50976 View 3D Structure Click here
P54715 View 3D Structure Click here
P54745 View 3D Structure Click here
P57437 View 3D Structure Click here
P57635 View 3D Structure Click here
P69786 View 3D Structure Click here
P69788 View 3D Structure Click here
P69826 View 3D Structure Click here
P69827 View 3D Structure Click here
P75039 View 3D Structure Click here
P75569 View 3D Structure Click here