O24993 (PLSX_HELPY) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphate acyltransferase
EC=2.3.1.n2

Alternative name(s):
Acyl-ACP phosphotransacylase
Acyl-[acyl-carrier-protein]--phosphate acyltransferase
Phosphate-acyl-ACP acyltransferase

Gene names

Name:	plsX
Ordered Locus Names:	HP_0201

Organism

Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori) [Reference proteome] [HAMAP]

Taxonomic identifier

85962 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › delta/epsilon subdivisions › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter › Helicobacter pylori

Protein attributes

Sequence length	337 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the reversible formation of acyl-phosphate (acyl-PO4) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA By similarity. HAMAP-Rule MF_00019
Catalytic activity	Acyl-[acyl-carrier-protein] + phosphate = acyl-phosphate + [acyl-carrier-protein]. HAMAP-Rule MF_00019
Pathway	Lipid metabolism; phospholipid metabolism. HAMAP-Rule MF_00019
Subunit structure	Homodimer. Probably interacts with PlsY By similarity.
Subcellular location	Cytoplasm By similarity. Note: Associated with the membrane possibly through PlsY By similarity.
Sequence similarities	Belongs to the PlsX family.
Sequence caution	The sequence AAD07269.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Lipid biosynthesis Lipid metabolism Phospholipid biosynthesis Phospholipid metabolism
Cellular component	Cytoplasm
Molecular function	Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	fatty acid biosynthetic process Inferred from electronic annotation. Source: HAMAP phospholipid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Inferred from electronic annotation. Source: InterPro transferase activity, transferring acyl groups other than amino-acyl groups 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 – 337	337	Phosphate acyltransferase HAMAP-Rule MF_00019		PRO_0000189887

Sequences

	Sequence		Length	Mass (Da)
	O24993 [UniParc]. Last modified May 30, 2000. Version 2. Checksum: 7916CD4F5911B23C	FASTA	337	36,352
	10 20 30 40 50 60 MKIVIDLMGA DHGVLPVIEG VSRALENKSF STVLVGDKDK ATPFISKELA SKVEMIHTQD 70 80 90 100 110 120 YIKMEEAATE AIKRKESSIY LGMDILKNGA DALISAGHSG ATMGLATLRL GRIKGVERPA 130 140 150 160 170 180 ICTLMPSVGK RPSVLLDAGA NTDCKPEYLI DFALMGYEYA KSVLHYDSPK VGLLSNGEED 190 200 210 220 230 240 IKGNMLVKET HKMLKAYDFF YGNVEGSDIF KGVVDVVVCD GFMGNVVLKT TEGVASAIGS 250 260 270 280 290 300 IFKDEIKSSF KSKMGALMLK NAFDILKQKT DYAEYGGAPL LGVNKSVIIS HGKSNARAIE 310 320 330 CAIYQAISAV ESQVCLRITQ AFESLKPSVS QSDQQDA

References

[1]

"The complete genome sequence of the gastric pathogen Helicobacter pylori." Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A., Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N., Loftus B.J., Richardson D.L., Dodson R.J. , Khalak H.G., Glodek A., McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E., Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D., Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S., Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C. Nature 388:539-547(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700392 / 26695.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000511 Genomic DNA. Translation: AAD07269.1. Different initiation.
PIR	A64545.
RefSeq	NP_207000.1. NC_000915.1. YP_006934124.1. NC_018939.1.
3D structure databases
ProteinModelPortal	O24993.
ModBase	Search...
Protein-protein interaction databases
STRING	85962.HP0201.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAD07269; AAD07269; HP_0201.
GeneID	13869380. 898919.
KEGG	heo:C694_01000. hpy:HP0201.
PATRIC	20591623. VBIHelPyl33062_0211.
Phylogenomic databases
eggNOG	COG0416.
KO	K03621.
OMA	DEKPSQA.
ProtClustDB	PRK05331.
Enzyme and pathway databases
UniPathway	UPA00085.
Family and domain databases
Gene3D	3.40.718.10. 1 hit.
HAMAP	MF_00019. PlsX.
InterPro	IPR003664. FA_synthesis. IPR024084. IsoPropMal-DH-like_dom. IPR012281. Phospholipid_synth_PlsX-like. [Graphical view]
Pfam	PF02504. FA_synthesis. 1 hit. [Graphical view]
PIRSF	PIRSF002465. Phsphlp_syn_PlsX. 1 hit.
TIGRFAMs	TIGR00182. plsX. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PLSX_HELPY

Accession

Primary (citable) accession number: O24993

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 30, 2000
Last modified:	May 1, 2013
This is version 75 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program