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Reviewed, UniProtKB/Swiss-Prot B7MJ31 (PLSB_ECO45)

Last modified October 13, 2009. Version 7. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Glycerol-3-phosphate acyltransferase
      Short name=GPAT
    EC=2.3.1.15
Gene names
Name: plsB
Ordered Locus Names: ECS88_4514
OrganismEscherichia coli O45:K1 (strain S88 / ExPEC) [Complete proteome] [HAMAP]
Taxonomic identifier585035 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length807 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

Acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol 3-phosphate. HAMAP MF_00393

Pathway

Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 1/3. HAMAP MF_00393

Subcellular location

Cell membrane; Peripheral membrane protein By similarity.

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 GPAT/DAPAT family.

Ontologies

Keywords
   Biological processPhospholipid biosynthesis
   Cellular componentCell membrane
Membrane
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processphospholipid biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Cellular componentextrinsic to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: HAMAP

   Molecular functionglycerol-3-phosphate O-acyltransferase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 807807Glycerol-3-phosphate acyltransferase HAMAP MF_00393
PRO_1000123075

Regions

Motif305 – 3106HXXXXD motif HAMAP MF_00393

Sequences

Sequence LengthMass (Da)Tools
B7MJ31-1 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: D6FC6892981D7EFE

FASTA80791,381
        10         20         30         40         50         60 
MSGWPRIYYK LLNLPLSILV KSKSIPADPA PELGLDTSRP IMYVLPYNSK ADLLTLRAQC 

        70         80         90        100        110        120 
LAHDLPDPLE PLEIDGTLLP RYVFIHGGPR VFTYYTPKEE SIKLFHDYLD LHRSNPNLDV 

       130        140        150        160        170        180 
QMVPVSVMFG RAPGREKGEV NPPLRMLNGV QKFFAVLWLG RDSFVRFSPS VSLRRMADEH 

       190        200        210        220        230        240 
GTDKTIAQKL ARVARMHFAR QRLAAVGPRL PARQDLFNKL LASRAIAKAV EDEARSKKIS 

       250        260        270        280        290        300 
HEKAQQNAIA LMEEIAANFS YEMIRLTDRI LGFTWNRLYQ GINVHNAERV RQLAHDGHEL 

       310        320        330        340        350        360 
VYVPCHRSHM DYLLLSYVLY HQGLVPPHIA AGINLNFWPA GPIFRRLGAF FIRRTFKGNK 

       370        380        390        400        410        420 
LYSTVFREYL GELFSRGYSV EYFVEGGRSR TGRLLDPKTG TLSMTIQAML RGGTRPITLI 

       430        440        450        460        470        480 
PIYIGYEHVM EVGTYAKELR GATKEKESLP QMLRGLSKLR NLGQGYVNFG EPMPLMTYLN 

       490        500        510        520        530        540 
QHVPDWRESI DPIEAVRPAW LTPTVNNIAA DLMVRINNAG AANAMNLCCT ALLASRQRSL 

       550        560        570        580        590        600 
TREQLTEQLN CYLDLMRNVP YSTDSTVPSA SASELIDHAL QMNKFEVEKD TIGDIIILPR 

       610        620        630        640        650        660 
EQAVLMTYYR NNIAHMLVLP SLMAAIVTQH RHISRDVLME HVNVLYPMLK AELFLRWDRD 

       670        680        690        700        710        720 
ELPDVIDALA NEMQRQGLIT LQDDELHINP AHSRTLQLLA AGARETLQRY AITFWLLSAN 

       730        740        750        760        770        780 
PSINRGTLEK ESRTVAQRLS VLHGINAPEF FDKAVFSSLV LTLRDEGYIS DSGDAEPAET 

       790        800 
MKVYQLLAEL ITSDVRLTIE SATQGEG 

« Hide

Cross-references

Sequence databases

CU928161 Genomic DNA. Translation: CAR05675.1.
RefSeqYP_002394024.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID7130380.
GenomeReviewsGene locus ECS88_4514 in contig CU928161_GR.

Organism-specific databases

CMRSearch...

Family and domain databases

HAMAPMF_00393.
[Tree]
InterProIPR002123. Acyltransferase.
[Graphical view]
PfamPF01553. Acyltransferase. 1 hit.
[Graphical view]
SMARTSM00563. PlsC. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePLSB_ECO45
AccessionPrimary (citable) accession number: B7MJ31
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: March 24, 2009
Last modified: October 13, 2009
This is version 7 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents