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Neisseria gonorrhoeae Search Results

Record: 1 of 1  
MiniMap IGR0510 IGR0508 IGR0511 IGR0509 IGR0512 IGR0514 IGR0507 IGR0513 NG0613 rsuA,psi, - NG0607 mltD, - NG0608 NG0609 plsC, - NG0611 fpg, - NG0610 rir2,nrdB, - NG0615 rir1,nrdA, - NG0614 NG0613 rsuA,psi, - NG0607 mltD, - NG0608 NG0609 plsC, - NG0611 fpg, - NG0610 rir2,nrdB, - NG0615 rir1,nrdA, - NG0614 NG0613 rsuA,psi, - NG0607 mltD, - NG0608 NG0609 plsC, - NG0611 fpg, - NG0610 rir2,nrdB, - NG0615 rir1,nrdA, - NG0614
* Calculated from Protein Sequence

Gene ID: NG0611

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
plsC  

Definition:
1-acyl-sn-glycerol-3-phosphate acyltransferase

Gene Start:
598437

Gene Stop:
599201

Gene Length:
765

Molecular Weight*:
27744

pI*:
10.40

Net Charge*:
12.24

EC:
2.3.1.51  

Functional Class:
Fatty acid and phospholipid metabolism; Biosynthesis  

Pathway: pathway table
Glycerolipid metabolism
Glycerophospholipid metabolism

Primary Evidence:
Swartley,J.S., Balthazar,J.T., Coleman,J., Shafer,W.M. and Stephens,D.S.,
Membrane glycerophospholipid biosynthesis in Neisseria meningitidis and Neisseria gonorrhoeae: identification, characterization, and mutagenesis of a lysophosphatidic acid acyltransferase,
Mol. Microbiol. 18 (3), 401-412 (1995)
Medline: 96342371.

Comment:
For other 'pls' genes see NG2171 (plsX).

From GenBANK (gi:3914395): This protein converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating acyl moiety at the 2 position. Catalytic activity: acyl-coa + 1-acyl-sn-glycerol 3-phosphate = coa + 1,2-diacyl-sn-glycerol 3-phosphate. This is the second step in de novo phospholipid biosynthesis. This protein is inner membrane-associated and belongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase family.

From Medline (96342371): Lysophosphatidic acid (LPA) acyltransferases of N.meningitidis and N.gonorrhoeae share homology with other prokaryotic and eukaryotic LPA acyltransferases. In E.coli, the conversion of LPA to phosphatidic acid, performed by the 1-acyl-sn-glycerol-3-phosphate acyltransferase PlsC, is a critical intermediate step in the biosynthesis of membrane glycerophospholipids. A Tn916-generated mutant of a serogroup B meningococcal strain was identified that exhibited increased amounts of capsular polysaccharide and a threefold increase in the number of assembled pili. In N.gonorrhoeae, the mutation increased piliation fivefold. The insertions were found to be within a gene that was subsequently designated nlaA (neisserial LPAacyltransferase). The predicted neisserial LPA acyltransferases were homologous (>20% identity, >40% amino acid similarity) to the family of PlsC protein homologues. The pathogenic Neisseria spp. appear to be able to utilize alternative enzyme(s) to produce phosphatidic acid. We postulate that the pathogenic Neisseria spp. are able to utilize alternate acyltransferases to produce glycerophospholipids in the absence of nlaA enzymatic activity. Implementation of these secondary enzymes results in alterations of glycerophospholipid composition that lead to pleiotropic effects on the cell surface components, including effects on capsule and piliation.

Oklahoma ID: NGO.611

Blast Summary:  PSI-Blast Search
NG0611 is 99% identical to a previously sequenced Neisseria gonorrhoeae 1-acyl-sn-glycerol-3-phosphate acyltransferase protein in GenBank, 972976, submitted by Swartley,J.S., Balthazar,J.T., Coleman,J., Shafer,W.M. and Stephens,D.S.

Many significant hits in gapped BLAST to 1-acylglycerol-3-phosphate O-acyltransferases and probable acyltransferases; e.g. residues 53-251 are 33% similar to AE004851, probable acyltransferase, of Pseudomonas aeruginosa.

Residues 1-255 are 97% similar to NMA1504, and are 96% similar to NMB1294, both 1-acyl-sn-glycerol-3-phosphate acyltransferases of N.meningitidis (gi12230452, gi12230455). Also similar to gi2120883.

COGS Summary:  COGS Search
BeTs to 11 clades of COG0204
COG name: 1-acyl-sn-glycerol-3-phosphate acyltransferase
Functional Class: I
The phylogenetic pattern of COG0204 is ----YQvCEbRhujgpolINX
Number of proteins in this genome belonging to this COG is 2

Blocks Summary:  Blocks Search
***** IPB002123 (Phospholipid and glycerol acyltransferase (from 'motifs_6msf')) with a combined E-value of 3.2e-06.
    IPB002123A    68-83
    IPB002123B    144-152


ProDom Summary:  Protein Domain Search
Residues 197-244 are identical to a (ACYLTRANSFERASE 1-ACYL-SN-GLYCEROL-3-PHOSPHATE) protein domain (PD036681) which is seen in PLSC_NEIGO.

Residues 71-196 are identical to a (ACYLTRANSFERASE TRANSFERASE PROTEIN PHOSPHOLIPID) protein domain (PD000989) which is seen in PLSC_NEIGO.

Residues 1-70 are 88% similar to a (ACYLTRANSFERASE 1-ACYL-SN-GLYCEROL-3-PHOSPHATE) protein domain (PD036683) which is seen in PLSC_NEIGO.



Paralogs:  Local Blast Search
NG0611 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.


Pfam Summary:  Pfam Search
Residues 60 to 182 (E-value = 7.1e-33) place NG0611 in the Acyltransferase family which is described as Acyltransferase (PF01553)

Structural Feature(s):
Feature Type  Start  Stop
transmembrane  
43  
59

PDB Hit:
No hits to the PDB database.

Gene Protein Sequence:
MSSNKASFFTRLRRLCRLTVWLFKTGKNLRGIDGGCPKSRNRAVIALGKG
ALAALDIGLEVGRPAPEHPNGVLVAANHVSWLDIFAMSAVYPSSFIAKQE
IKSWPVLGKMGQNAGTVFINRNSRRDIEPINRAVCETLQRGQNVSFFPEA
RTSSGLGLLPFKAALFQSAIDAGAKVLAVALRYYDETGKRTARPSYADVG
LPTCLWRIVSMKKLTIKVDFVCVADAAESEDRYALKDKIEESIRAVVAGD
ADVAV

Gene Nucleotide Sequence:  Sequence Viewer
ATGTCTTCAAATAAAGCTTCATTTTTTACACGTCTGCGCCGCTTGTGCCG
CTTGACGGTCTGGCTGTTCAAAACCGGCAAAAACCTGCGCGGTATTGACG
GCGGCTGCCCCAAGTCGCGCAATCGGGCAGTTATAGCGTTGGGCAAGGGC
GCTTTGGCGGCTTTGGATATCGGATTGGAGGTGGGCAGACCCGCACCCGA
ACATCCGAACGGTGTCTTGGTTGCCGCCAACCACGTGTCCTGGCTGGATA
TTTTCGCGATGAGCGCGGTTTATCCGAGTAGCTTTATCGCCAAGCAGGAA
ATCAAAAGCTGGCCGGTATTGGGCAAGATGGGGCAGAACGCGGGAACGGT
GTTCATCAACCGCAATTCGCGGCGCGACATCGAACCGATTAACCGCGCCG
TCTGCGAAACCTTGCAACGCGGTCAAAACGTCAGTTTTTTCCCTGAGGCG
CGAACTTCCTCCGGACTGGGGCTCCTGCCGTTCAAGGCTGCGCTGTTCCA
ATCCGCCATCGATGCGGGGGCAAAGGTTTTGGCGGTCGCACTGCGTTATT
ATGACGAAACGGGAAAAAGGACGGCCCGTCCGTCGTATGCCGATGTCGGT
TTGCCGACTTGCCTGTGGCGAATCGTGTCTATGAAAAAACTGACTATCAA
AGTCGATTTCGTTTGCGTGGCGGACGCGGCGGAAAGCGAAGACCGTTATG
CTTTAAAAGATAAAATCGAAGAAAGCATCCGTGCCGTTGTCGCAGGCGAT
GCGGATGTTGCCGTC


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