| General information | | DisProt: | DP00529 | | Name: | Plasmid partition protein ParG | | Synonym(s): | Q9KJ82_SALNE
| | First appeared in release: | Release 3.7 (01/28/2008) | | UniProt: | Q9KJ82 | | UniGene: | | | SwissProt: | Q9KJ82_SALNE | | TrEMBL: | | | NCBI (GI): | 8272472 | | Source organism: | Salmonella enterica (serovar Newport) | | Sequence length: | 76 | | Percent disordered: | 42% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MSLEKAHTSV KKMTFGENRD LERVVTAPVS SGKIKRVNVN FDEEKHTRFK AACARKGTSI - 60
TDVVNQLVDN WLKENE
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| Functional narrative |
ParG is the prototype of a group of small (<10 kDa) proteins involved in accurate plasmid segregation. The protein is a dimeric DNA binding factor, which consists of symmetric paired C-terminal domains that interleave into a ribbon-helix-helix fold that is crucial for the interaction with DNA, and unstructured N-terminal domains. The flexible tails modulate the organization of a higher order nucleoprotein complex that is crucial for proper transcriptional repression. This is achieved by transient associations between the flexible and folded domains in complex with the target DNA.
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered | | Name: | | | Location: | 1 - 32 | | Length: | 32 | | Region sequence: |
MSLEKAHTSVKKMTFGENRDLERVVTAPVSSG | | Modification type: | Native
| | PDB: | | | Structural/functional type: | | | Functional classes: | | | Functional subclasses: | | Detection methods:
| References:
- Carmelo E, Barillà D, Golovanov AP, Lian LY, Derome A, Hayes F. "The unstructured N-terminal tail of ParG modulates assembly of a quaternary nucleoprotein complex in transcription repression." J Biol Chem. 2005; 280(31): 28683-91. PubMed: 15951570
| Comments:
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| References |
- Golovanov AP, Barillà D, Golovanova M, Hayes F, Lian LY. "ParG, a protein required for active partition of bacterial plasmids, has a dimeric ribbon-helix-helix structure." Mol Microbiol. 2003; 50(4): 1141-53. PubMed: 14622405
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