Detailed information of oriT
oriT
The information of the oriT region
| oriTDB ID | 100183 |
| Name | oriT_pMV158  |
| Organism | Streptococcus agalactiae |
| Sequence Completeness | core |
| NCBI accession of oriT (coordinates [strand]) | NC_010096 (3570..3610 [+], 41 nt) |
| oriT length | 41 nt |
| IRs (inverted repeats) | 2..8, 13..19 (ACTTTAT..ATAAAGT) |
| Location of nic site | 27..28 |
| Conserved sequence flanking the nic site |
TAGTGTG|TTAT |
| Note | (1) The relaxase MobM_pMV158 activity is dependent on Mn2+ or Mg2+ [PMID:21296755]. (2) Mn2+, but ont Mg2+, can promote the thermal stability of the relaxase MobM_pMV158. [PMID:21296755]. (3) The relaxase MobM_pMV158 exhibited a high affinity binding for Mn2+ but not for Mg2+ [PMID:21296755]. (4) The relaxase MobM_pMV158 is a dimer with an ellipsoidal shape, and it is associated with the cell membrane [PMID:14687570]. (5) The relaxase MobM_pMV158, by recognizing the oriTpMV158 IR2 sequences, can mediate a hairpin extrusion conformational change in oriTpMV158. In this way, the relaxase MobM_pMV158 can act as a molecular switch on controling the mobilization of pMV158 [PMID:29600250]. (6) The relaxase MobM_pMV158 use a histidine (H22) as catalytic residue, not the commonly used tyrosine residue by other relaxase families [PMID:28739894]. (7) The N-terminal construct of the first 243 amino acid residues within the relaxase MobM_pMV158 is capable of nicking the DNA substrate independently of its topology [PMID:14687570]. (8) The amino acids 200 to 243 of the relaxase MobM_pMV158 modulate substrate specificity but not the nicking activity per se [PMID:14687570]. |
oriT sequence
Download Length: 41 nt
CACTTTATGAATATAAAGTATAGTGTGTTATACTTTACATG
Visualization of oriT structure (The oriT was characterized experimentally)
oriT secondary structure
Predicted by RNAfold.
Download structure file
Reference
[1] Alippi AM et al. (2014) Tetracycline-resistance encoding plasmids from Paenibacillus larvae, the causal agent of American foulbrood disease, isolated from commercial honeys. Int Microbiol. 17(1):49-61. [PMID:25296446]
[2] Tomita H et al. (2005) Genetic analysis of transfer-related regions of the vancomycin resistance Enterococcus conjugative plasmid pHTbeta: identification of oriT and a putative relaxase gene. J Bacteriol. 187(22):7727-37. [PMID:16267297]
[3] Francia MV et al. (2004) A classification scheme for mobilization regions of bacterial plasmids. FEMS Microbiol Rev. 28(1):79-100. [PMID:14975531]
[4] Grohmann E et al. (2003) Conjugative plasmid transfer in gram-positive bacteria. Microbiol Mol Biol Rev. 67(2):277-301. [PMID:12794193]
[5] Turgeon N et al. (2001) Isolation and characterization of a Streptococcus thermophilus plasmid closely related to the pMV158 family. Plasmid. 45(3):171-83. [PMID:11407913]
[6] Farías ME et al. (2000) Conjugal transfer of plasmid pMV158: uncoupling of the pMV158 origin of transfer from the mobilization gene mobM, and modulation of pMV158 transfer in Escherichia coli mediated by IncP plasmids. Microbiology. 146 (Pt 9):2259-65. [PMID:10974113]
[7] Grohmann E et al. (1999) Mobilisation of the streptococcal plasmid pMV158: interactions of MobM protein with its cognate oriT DNA region. Mol Gen Genet. 261(4-5):707-15. [PMID:10394908]
[8] Guzmán LM et al. (1997) The mobilization protein, MobM, of the streptococcal plasmid pMV158 specifically cleaves supercoiled DNA at the plasmid oriT. Mol Gen Genet. 266(4):688-702. [PMID:9102462]
[9] Priebe SD et al. (1989) Region of the streptococcal plasmid pMV158 required for conjugative mobilization. J Bacteriol. 171(9):4778-84. [PMID:2768188]
Relaxase
| ID | 176 | GenBank | YP_001586274 |
| Name | MobM_pMV158 |
UniProt ID | P13925 |
| Length | 494 a.a. | PDB ID | |
| Note | (1) The relaxase MobM_pMV158 activity is dependent on Mn2+ or Mg2+ [PMID:21296755]. (2) Mn2+, but ont Mg2+, can promote the thermal stability of the relaxase MobM_pMV158. [PMID:21296755]. (3) The relaxase MobM_pMV158 exhibited a high affinity binding for Mn2+ but not for Mg2+ [PMID:21296755]. (4) The relaxase MobM_pMV158 is a dimer with an ellipsoidal shape, and it is associated with the cell membrane [PMID:14687570]. (5) The relaxase MobM_pMV158, by recognizing the oriTpMV158 IR2 sequences, can mediate a hairpin extrusion conformational change in oriTpMV158. In this way, the relaxase MobM_pMV158 can act as a molecular switch on controling the mobilization of pMV158 [PMID:29600250]. (6) The relaxase MobM_pMV158 use a histidine (H22) as catalytic residue, not the commonly used tyrosine residue by other relaxase families [PMID:28739894]. (7) The N-terminal construct of the first 243 amino acid residues within the relaxase MobM_pMV158 is capable of nicking the DNA substrate independently of its topology [PMID:14687570]. (8) The amino acids 200 to 243 of the relaxase MobM_pMV158 modulate substrate specificity but not the nicking activity per se [PMID:14687570]. |
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Relaxase protein sequence
Download Length: 494 a.a. Molecular weight: 57859.44 Da Isoelectric Point: 6.5216
MSYMVARMQKMKAGNLGGAFKHNERVFETHSNKDINPSRSHLNYELTDRDRSVSYEKQIKDYVNENKVSN
RAIRKDAVLCDEWIITSDKDFFEKLDEEQTRTFFETAKNYFAENYGESNIAYASVHLDESTPHMHMGVVP
FENGKLSSKAMFDREELKHIQEDLPRYMSDHGFELERGKLNSEAKHKTVAEFKRAMADMELKEELLEKYH
APPFVDERTGELNNDTEAFWHEKEFADMFEVQSPIRETTNQEKMDWLRKQYQEELKKLESSKKPLEDDLS
HLEELLDKKTKEYIKIDSEASERASELSKAEGYINTLENHSKSLEAKIECLESDNLQLEKQKATKLEAKA
LNESELRELKPKKNFLGKEHYELSPEQFEGLKAEVYRSRTLLHHKDIELEQAKRQVSLRASKNYFTASLE
RAKEKAKGESIDRLKSEIKRLKNENSILRQQNDKMLGKLRELMPDKAFKNLLSELKAIKPIVNIIKKAIE
KSLF
Protein domains
Predicted by InterproScan.
Protein structure
| Source | ID | Structure |
|---|---|---|
| PDB | 4LVI | |
| PDB | 4LVJ | |
| PDB | 4LVK | |
| PDB | 4LVL | |
| PDB | 4LVM | |
| AlphaFold DB | P13925 |
Reference
[1] Grohmann E et al. (2003) Conjugative plasmid transfer in gram-positive bacteria. Microbiol Mol Biol Rev. 67(2):277-301. [PMID:12794193]
[2] Farías ME et al. (2000) Conjugal transfer of plasmid pMV158: uncoupling of the pMV158 origin of transfer from the mobilization gene mobM, and modulation of pMV158 transfer in Escherichia coli mediated by IncP plasmids. Microbiology. 146 (Pt 9):2259-65. [PMID:10974113]
[3] Grohmann E et al. (1999) Mobilisation of the streptococcal plasmid pMV158: interactions of MobM protein with its cognate oriT DNA region. Mol Gen Genet. 261(4-5):707-15. [PMID:10394908]
[4] Guzmán LM et al. (1997) The mobilization protein, MobM, of the streptococcal plasmid pMV158 specifically cleaves supercoiled DNA at the plasmid oriT. Mol Gen Genet. 266(4):688-702. [PMID:9102462]
[5] Priebe SD et al. (1989) Region of the streptococcal plasmid pMV158 required for conjugative mobilization. J Bacteriol. 171(9):4778-84. [PMID:2768188]
Host bacterium
| ID | 176 | GenBank | NC_010096 |
| Plasmid name | pMV158 | Incompatibility group | - |
| Plasmid size | 5541 bp | Coordinate of oriT [Strand] | 3570..3610 [+] |
| Host baterium | Streptococcus agalactiae |
Cargo genes
| Drug resistance gene | tet(L) |
| Virulence gene | - |
| Metal resistance gene | - |
| Degradation gene | - |
| Symbiosis gene | - |
| Anti-CRISPR | - |