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Mycoplasma genitalium Search Results

Record: 1 of 1  
MiniMap IGR152 IGR155 IGR151 IGR150 lsp, - MG210 rluD, - MG209 hrcA, - MG205 MG211.1 MG207 MG211 MG210.1 pfk, - MG215 uvrC, - MG206 MG213 lsp, - MG210 rluD, - MG209 hrcA, - MG205 MG211.1 MG207 MG211 MG210.1 pfk, - MG215 uvrC, - MG206 MG213 lsp, - MG210 rluD, - MG209 hrcA, - MG205 MG208 MG208 MG207 MG211 MG210.1 uvrC, - MG206 MG213 MG214 plsC, - MG212 plsC, - MG212 pfk, - MG215 MG211.1 MG214
* Calculated from Protein Sequence

Gene ID: MG210

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
lsp  

Definition:
prolipoprotein signal peptidase

Gene Start:
249947

Gene Stop:
249405

Gene Length:
543

Molecular Weight*:
20825

pI*:
10.33

Net Charge*:
8.32

EC:
3.4.23.36  3.4.99.-  

Functional Class:
Cellular processes; Protein and peptide secretion  

Pathway: pathway table
Miscellaneous enzymes

Secondary Evidence:
Sankaran K, Wu HC. 1995. Bacterial prolipoprotein signal peptidase. Methods Enzymol 248:169-80. Medline: 7674920.

Munoa FJ, Miller KW, Beers R, Graham M, Wu HC. 1991. Membrane topology of Escherichia coli prolipoprotein signal peptidase (signal peptidase II). J Biol Chem 266(26):17667-72. Medline: 1894646.

Yamagata H . 1983. Temperature-sensitive prolipoprotein signal peptidase in an Escherichia coli mutant: use of the mutant for an efficient and convenient assay system. J Biochem (Tokyo) 93(6):1509-15. Medline: 6350278.

Comment:
The LspA protein is thought to be an integral membrane peptidase, responsible for cleavage of N-terminal leader sequences from prolipoproteins.

In E. coli, globomycin inhibits prolipoprotein signal peptidase (Dev, IK et al., 1985. Medline: 3888977). The prolipoprotein signal peptidase in E. coli is transcribed on the same mRNA as ileS (isoleucyl-tRNA synthetase; Miller and Wu, 1987. Medline: 2432063; Tokunaga M, et al., 1985. Medline: 258083).


Blast Summary:  PSI-Blast Search
Hits in gapped BLAST to predicted mycoplasma prolipoprotein signal
peptidase sequences, e.g. residues 8-180 are 62% similar to LSPA_MYCPN.

MG210 is orthologously related to MP0542: residues 8-180 of MG210 are 69% similar to residues 7-184 of MP0542, a predicted prolipoprotein signal peptidase from M. pneumoniae. MG210 is also similar to a predicted prolipoprotein signal peptidase from U. urealyticum, UU314. No significant similarities to C. trachomatis, C. pneumoniae or T. pallidum sequences.

COGS Summary:  COGS Search
The phylogenetic pattern of COG0597 is ehgpc---.
COG name: Prolipoprotein signal peptidase.
Functional Class: N
BeTs to e-g-c---.


Blocks Summary:  Blocks Search
Residues 65-88, 112-137, 146-165 are members of blocks BL00855A-C (signal
peptidases).

ProDom Summary:  Protein Domain Search
Residues 28-145 are 28% similar to a urease-related domain as seen in
URED_HELPY.

Paralogs:  Local Blast Search
No evidence of paralogs in M. genitalium.

Pfam Summary:  Pfam Search
Residues 28 to 176 (E-value = 3.4e-68) place MG210 in the Peptidase_A8 family which is described as Signal peptidase (SPase) II (PF01252)

Structural Feature(s):
Feature Type  Start  Stop
transmembrane  
27  
46
transmembrane  
86  
120
transmembrane  
150  
171

PDB Hit:


Gene Protein Sequence:
MKLRKTKFFSQLKHQVLTANQKPFLFYKLTMIGFVGFIILLQVFILRNAL
NGEMDNTMVANSGFINIYVIRNKGVGFSLLQNQTGLVYFLQGLLSVIALV
FLVFMVKYSYIFWITTLAFGSLGNFFDRLTSANDSVLDYFIFQNGSSVFN
FADCCITFGFIGLFFCFLIQMFKEFKHSKNQ

Gene Nucleotide Sequence:  Sequence Viewer
ATGAAATTAAGAAAAACCAAGTTTTTTTCACAACTTAAACACCAGGTTTT
AACTGCAAACCAAAAACCATTTTTATTCTATAAACTGACAATGATTGGGT
TTGTTGGCTTTATTATCTTACTGCAAGTTTTCATATTAAGAAATGCGTTA
AATGGTGAGATGGATAACACCATGGTAGCAAATAGTGGTTTTATTAATAT
CTATGTGATTAGAAACAAAGGGGTAGGGTTTAGCTTATTACAAAACCAAA
CTGGCTTAGTTTACTTTCTCCAGGGATTATTATCAGTAATTGCGTTAGTT
TTTCTTGTTTTTATGGTGAAATATAGTTACATCTTTTGAATTACAACTTT
AGCATTTGGTTCACTTGGAAACTTCTTTGATCGTTTAACTTCAGCTAATG
ATTCAGTGTTAGATTACTTTATCTTTCAGAATGGTAGTTCAGTATTTAAC
TTTGCTGATTGTTGTATTACCTTTGGTTTTATAGGTTTATTCTTTTGTTT
TTTAATCCAGATGTTCAAAGAGTTTAAACATTCCAAAAACCAG


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