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Q83R47 (PGSA_SHIFL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase

EC=2.7.8.5
Alternative name(s):
Phosphatidylglycerophosphate synthase
Short name=PGP synthase
Gene names
Name:pgsA
Ordered Locus Names:SF1955, S2051
OrganismShigella flexneri [Complete proteome] [HAMAP]
Taxonomic identifier623 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella

Protein attributes

Sequence length182 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred 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.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 182181CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase HAMAP MF_01437
PRO_0000239131

Regions

Topological domain2 – 1211Cytoplasmic Potential
Transmembrane13 – 3725Helical; Potential
Topological domain38 – 6023Periplasmic Potential
Transmembrane61 – 8121Helical; Potential
Topological domain82 – 865Cytoplasmic Potential
Transmembrane87 – 10721Helical; Potential
Topological domain108 – 14538Periplasmic Potential
Transmembrane146 – 16823Helical; Potential
Topological domain169 – 18113Cytoplasmic Potential

Sequences

Sequence LengthMass (Da)Tools
Q83R47 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: A6E0502ABE6DDEA4

FASTA18220,729
        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 YVGIALFFVA AVLTLWSMLQ YLSAARADLL 


DQ 

« Hide

References

[1]"Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157."
Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y. expand/collapse author list , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.
Nucleic Acids Res. 30:4432-4441(2002) [PubMed: 12384590] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 301 / Serotype 2a.
[2]"Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T."
Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.
Infect. Immun. 71:2775-2786(2003) [PubMed: 12704152] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700930 / 2457T / Serotype 2a.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005674 Genomic DNA. Translation: AAN43506.1.
AE014073 Genomic DNA. Translation: AAP17336.1.
RefSeqNP_707799.1. NC_004337.2.
NP_837527.1. NC_004741.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000086621; EBESCP00000083443; EBESCG00000085666.
EBESCT00000092789; EBESCP00000089425; EBESCG00000091833.
GeneID1025192.
1078369.
GenomeReviewsGene locus SF1955 in contig AE005674_GR.
Gene locus S2051 in contig AE014073_GR.
KEGGsfl:SF1955.
sfx:S2051.
PATRIC18705574. VBIShiFle31049_2275.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000009502.
HOGENOMHBG686655.
OMAWSYMAAS.
ProtClustDBPRK10832.

Enzyme and pathway databases

BioCycSFLE198214:AAN43506.1-MONOMER.

Family and domain databases

HAMAPMF_01437. PgsA.
[Tree]
InterProIPR000462. CDP-OH_P_trans.
IPR023762. PGP_synthase_bac.
IPR004570. Phosphatidylglycerol_P_synth.
[Graphical view]
KOK00995.
PfamPF01066. CDP-OH_P_transf. 1 hit.
[Graphical view]
PIRSFPIRSF000847. Phos_ph_gly_syn. 1 hit.
TIGRFAMsTIGR00560. PgsA. 1 hit.
PROSITEPS00379. CDP_ALCOHOL_P_TRANSF. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePGSA_SHIFL
AccessionPrimary (citable) accession number: Q83R47
Secondary accession number(s): Q7C173
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 73 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families