Reviewed, UniProtKB/Swiss-Prot Q59601 (PLSC_NEIGO)

Names and origin

Protein names

Recommended name:
    1-acyl-sn-glycerol-3-phosphate acyltransferase
      Short name=1-AGP acyltransferase
      Short name=1-AGPAT
    EC=2.3.1.51
Alternative name(s):
    Lysophosphatidic acid acyltransferase
      Short name=LPAAT

Gene names

Name:

plsC

Organism

Neisseria gonorrhoeae

Taxonomic identifier

485 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria

Protein attributes

Sequence length	255 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	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.
Pathway	Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
Subcellular location	Cell inner membrane; Peripheral membrane protein.
Domain	The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate By similarity.
Sequence similarities	Belongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase family.

Ontologies

Keywords
Biological process	Phospholipid biosynthesis
Cellular component	Cell inner membrane Cell membrane Membrane
Molecular function	Acyltransferase Transferase
Gene Ontology (GO)
Biological process	phospholipid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	1-acylglycerol-3-phosphate O-acyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 255	255	1-acyl-sn-glycerol-3-phosphate acyltransferase		PRO_0000208174
Regions
	Motif	78 – 83	6	HXXXXD motif

Sequences

	Sequence		Length	Mass (Da)
	Q59601-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 833F080361A5CE88	FASTA	255	27,830
	10 20 30 40 50 60 MSSNKASFFT RLRRLCRLTV WLFKTGKNLR GIDGGCPKSR NRAVIALGKG ALAALDIGLE 70 80 90 100 110 120 VGRPAPEHPN GVLVAANHVS WLDIFAMSAV YPSSFIAKQE IKSWPVLGKM GQNAGTVFIN 130 140 150 160 170 180 RNSRRDIEPI NRAVCETLQR GQNVSFFPEA RTSSGLGLLP FKAALFQSAI DAGAKVLAVA 190 200 210 220 230 240 LRYYDETGKR TARPSYADVG LPTCLWRIVS MKKLTIKVDF VCVADAAESE DRYALKDKIE 250 ESIRAVVADD ADIAV

References

[1]

"Membrane glycerophospholipid biosynthesis in Neisseria meningitidis and Neisseria gonorrhoeae: identification, characterization, and mutagenesis of a lysophosphatidic acid acyltransferase." Swartley J.S., Balthazar J.T., Coleman J., Shafer W.M., Stephens D.S. Mol. Microbiol. 18:401-412(1995) [PubMed: 8748025] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: FA19.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U21806 Genomic DNA. Translation: AAB40877.1.
PIR	S70545.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	2.3.1.51. 588.
Family and domain databases
InterPro	IPR002123. Acyltransferase. IPR004552. AGP_acyltrans. [Graphical view]
Pfam	PF01553. Acyltransferase. 1 hit. [Graphical view]
SMART	SM00563. PlsC. 1 hit. [Graphical view]
TIGRFAMs	TIGR00530. AGP_acyltrn. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PLSC_NEIGO

Accession

Primary (citable) accession number: Q59601

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	November 1, 1996
Last modified:	October 13, 2009
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)