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P58130 (PLSB_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 69. 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:
Glycerol-3-phosphate acyltransferase

Short name=GPAT
EC=2.3.1.15
Gene names
Name:plsB
Ordered Locus Names:Z5640, ECs5024
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length807 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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 inner membrane; Peripheral membrane protein; Cytoplasmic side By similarity HAMAP MF_00393.

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. HAMAP MF_00393

Sequence similarities

Belongs to the GPAT/DAPAT family.

Sequence caution

The sequence AAG59240.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAB38447.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentplasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionglycerol-3-phosphate O-acyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 807806Glycerol-3-phosphate acyltransferase HAMAP MF_00393
PRO_0000195220

Regions

Motif306 – 3116HXXXXD motif HAMAP MF_00393

Sequences

Sequence LengthMass (Da)Tools
P58130 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 26FC7F929639F593

FASTA80791,409
        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 VHSRTLQLLA AGARETLQRY AITFWLLSAN 

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

       790        800 
MKVYQLLAEL ITSDVRLTIE SATQGEG 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005174 Genomic DNA. Translation: AAG59240.1. Different initiation.
BA000007 Genomic DNA. Translation: BAB38447.1. Different initiation.
PIRD86097.
H91256.
RefSeqNP_290675.2. NC_002655.2.
NP_313051.2. NC_002695.1.

3D structure databases

ProteinModelPortalP58130.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000026259; EBESCP00000025152; EBESCG00000025312.
EBESCT00000057388; EBESCP00000055216; EBESCG00000056436.
GeneID915055.
960082.
GenomeReviewsGene locus Z5640 in contig AE005174_GR.
Gene locus ECs5024 in contig BA000007_GR.
KEGGece:Z5640.
ecs:ECs5024.
PATRIC18359643. VBIEscCol44059_4958.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000010697.
HOGENOMHBG296590.
OMAWNKLYQG.
ProtClustDBPRK04974.

Enzyme and pathway databases

BioCycECOL83334:ECS5024-MONOMER.

Family and domain databases

HAMAPMF_00393. Glyc3P_acyltrans.
[Tree]
InterProIPR002123. Acyltransferase.
IPR022284. G3P_O-AcylTrfase.
[Graphical view]
KOK00631.
PfamPF01553. Acyltransferase. 1 hit.
[Graphical view]
PIRSFPIRSF000437. GPAT_DHAPAT. 1 hit.
SMARTSM00563. PlsC. 1 hit.
[Graphical view]
TIGRFAMsTIGR03703. PlsB. 1 hit.
ProtoNetSearch...

Entry information

Entry namePLSB_ECO57
AccessionPrimary (citable) accession number: P58130
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 69 of the entry and version 2 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