Detailed information of relaxase

Relaxase

• ID: 176
• GenBank: YP_001586274
• Name: MobM_pMV158
• UniProt ID: P13925
• Family: MOB_V
• PDB ID: 4LVI, 4LVJ, 4LVK, 4LVL, 4LVM
• Length: 494 a.a.
• 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].

Protein sequence

• Length: 494 a.a.
• Molecular weight: 57859.44 Da
• Isoelectric Point: 6.5216

>YP_001586274.1 unnamed protein product (plasmid) [Streptococcus agalactiae]
MSYMVARMQKMKAGNLGGAFKHNERVFETHSNKDINPSRSHLNYELTDRDRSVSYEKQIKDYVNENKVSN
RAIRKDAVLCDEWIITSDKDFFEKLDEEQTRTFFETAKNYFAENYGESNIAYASVHLDESTPHMHMGVVP
FENGKLSSKAMFDREELKHIQEDLPRYMSDHGFELERGKLNSEAKHKTVAEFKRAMADMELKEELLEKYH
APPFVDERTGELNNDTEAFWHEKEFADMFEVQSPIRETTNQEKMDWLRKQYQEELKKLESSKKPLEDDLS
HLEELLDKKTKEYIKIDSEASERASELSKAEGYINTLENHSKSLEAKIECLESDNLQLEKQKATKLEAKA
LNESELRELKPKKNFLGKEHYELSPEQFEGLKAEVYRSRTLLHHKDIELEQAKRQVSLRASKNYFTASLE
RAKEKAKGESIDRLKSEIKRLKNENSILRQQNDKMLGKLRELMPDKAFKNLLSELKAIKPIVNIIKKAIE
KSLF

Protein domains

Predicted by InterproScan

• Plasmid recombination enzyme (Mob_Pre) (1-193)

Protein 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]