C6UYB5 (C6UYB5_ECO5T) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase HAMAP MF_01437
EC=2.7.8.5 HAMAP MF_01437

Alternative name(s):
Phosphatidylglycerophosphate synthase HAMAP MF_01437

Gene names

Name:	pgsA HAMAP MF_01437 EMBL ACT72323.1
Ordered Locus Names:	ECSP_2516

Organism

Escherichia coli O157:H7 (strain TW14359 / EHEC) [Complete proteome] [HAMAP]

Taxonomic identifier

544404 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	182 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	This protein catalyzes the committed step to the synthesis of the acidic phospholipids By similarity. HAMAP MF_01437
Catalytic activity	CDP-diacylglycerol + sn-glycerol 3-phosphate = CMP + 3(3-sn-phosphatidyl)-sn-glycerol 1-phosphate. HAMAP MF_01437
Pathway	Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 1/2. HAMAP MF_01437
Subcellular location	Cell inner membrane; Multi-pass membrane protein By similarity HAMAP MF_01437.
Sequence similarities	Belongs to the CDP-alcohol phosphatidyltransferase class-I family. HAMAP MF_01437 RuleBase RU003750

Ontologies

Keywords
Biological process	Phospholipid biosynthesis HAMAP MF_01437
Cellular component	Cell inner membrane HAMAP MF_01437 Cell membrane Membrane
Domain	Transmembrane Transmembrane helix HAMAP MF_01437
Molecular function	Transferase HAMAP MF_01437 RuleBase RU003750
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	phospholipid biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Regions
	Topological domain	1 – 12	12	Cytoplasmic By similarity HAMAP MF_01437
	Transmembrane	13 – 37	25	Helical; By similarity HAMAP MF_01437
	Topological domain	38 – 60	23	Periplasmic By similarity HAMAP MF_01437
	Transmembrane	61 – 81	21	Helical; By similarity HAMAP MF_01437
	Topological domain	82 – 86	5	Cytoplasmic By similarity HAMAP MF_01437
	Transmembrane	87 – 107	21	Helical; By similarity HAMAP MF_01437
	Topological domain	108 – 145	38	Periplasmic By similarity HAMAP MF_01437
	Transmembrane	146 – 168	23	Helical; By similarity HAMAP MF_01437
	Topological domain	169 – 181	13	Cytoplasmic By similarity HAMAP MF_01437

Sequences

	Sequence		Length	Mass (Da)
	C6UYB5 [UniParc]. Last modified September 22, 2009. Version 1. Checksum: F8F0502ABE6DC8D5	FASTA	182	20,701
	10 20 30 40 50 60 MQFNIPTLLT LFRVILIPFF VLVFYLPVTW SPFAAALIFC VAAVTDWFDG FLARRWNQST 70 80 90 100 110 120 RFGAFLDPVA DKVLVAIAMV LVTEHYHSWW VTLPAATMIA REIIISALRE WMAELGKRSS 130 140 150 160 170 180 VAVSWIGKVK TTAQMVALAW LLWRPNIWVE YAGIALFFVA AVLTLWSMLQ YLSAARADLL DQ

References

[1]

"Analysis of the genome of the Escherichia coli O157:H7 2006 spinach-associated outbreak isolate indicates candidate genes that may enhance virulence." Kulasekara B.R., Jacobs M., Zhou Y., Wu Z., Sims E., Saenphimmachak C., Rohmer L., Ritchie J.M., Radey M., McKevitt M., Freeman T.L., Hayden H., Haugen E., Gillett W., Fong C., Chang J., Beskhlebnaya V., Waldor M.K. , Samadpour M., Whittam T.S., Kaul R., Brittnacher M., Miller S.I. Infect. Immun. 77:3713-3721(2009) [PubMed: 19564389] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001368 Genomic DNA. Translation: ACT72323.1.
RefSeq	YP_003078399.1. NC_013008.1.
3D structure databases
ProteinModelPortal	C6UYB5.
ModBase	Search...
Protein-protein interaction databases
STRING	C6UYB5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000166623; EBESCP00000156760; EBESCG00000166520.
GeneID	8217082.
GenomeReviews	Gene locus ECSP_2516 in contig CP001368_GR.
KEGG	etw:ECSP_2516.
PATRIC	18389066. VBIEscCol9396_2575.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000009502.
OMA	WSYMAAS.
ProtClustDB	PRK10832.
Family and domain databases
HAMAP	MF_01437. PgsA. [Tree]
InterPro	IPR000462. CDP-OH_P_trans. IPR023762. PGP_synthase_bac. IPR004570. Phosphatidylglycerol_P_synth. [Graphical view]
KO	K00995.
Pfam	PF01066. CDP-OH_P_transf. 1 hit. [Graphical view]
PIRSF	PIRSF000847. Phos_ph_gly_syn. 1 hit.
TIGRFAMs	TIGR00560. PgsA. 1 hit.
PROSITE	PS00379. CDP_ALCOHOL_P_TRANSF. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

C6UYB5_ECO5T

Accession

Primary (citable) accession number: C6UYB5

Entry history

Integrated into UniProtKB/TrEMBL:	September 22, 2009
Last sequence update:	September 22, 2009
Last modified:	December 14, 2011
This is version 20 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)