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Protein

Lipid A palmitoyltransferase PagP

Gene

pagP

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Transfers a palmitate residue from the sn-1 position of a phospholipid to the N-linked hydroxymyristate on the proximal unit of lipid A or its precursors. Phosphatidylglycerol (PtdGro), phosphatidylethanolamine (PtdEtn), phosphatidylserine (PtdSer) and phosphatidic acid (Ptd-OH) are all effective acyl donors.3 Publications

Miscellaneous

Overproduction leads to camphor resistance and chromosome condensation.1 Publication

Catalytic activityi

1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine + hexa-acyl lipid A = 2-acyl-sn-glycero-3-phosphocholine + hepta-acyl lipid A.UniRule annotation1 Publication
1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine + lipid II(A) = 2-acyl-sn-glycero-3-phosphocholine + lipid II(B).UniRule annotation
1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine + lipid IV(A) = 2-acyl-sn-glycero-3-phosphocholine + lipid IV(B).UniRule annotation1 Publication

Activity regulationi

Inhibited by lauryldimethylamine oxide (LDAO) and dodecylphosphocholine (DPC).1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei58UniRule annotation2 Publications1
Sitei67Role in lipopolysaccharide recognitionUniRule annotation1
Active sitei101UniRule annotation2 Publications1
Active sitei102UniRule annotation2 Publications1
Sitei172Role in the phospholipid gatingUniRule annotation1

GO - Molecular functioni

  • O-palmitoyltransferase activity Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionAcyltransferase, Transferase

Enzyme and pathway databases

BioCyciEcoCyc:EG12180-MONOMER
MetaCyc:EG12180-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
Lipid A palmitoyltransferase PagPUniRule annotationCurated (EC:2.3.1.251UniRule annotation1 Publication)
Alternative name(s):
Lipid A acylation proteinUniRule annotation
Gene namesi
Name:pagPUniRule annotation
Synonyms:crcA1 Publication, ybeG
Ordered Locus Names:b0622, JW0617
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12180 pagP

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cell outer membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi58H → F: Drastically reduces palmitoyltransferase activity while leaving expression and membrane insertion intact. 1 Publication1
Mutagenesisi58H → N: Drastically reduces palmitoyltransferase activity while leaving expression and membrane insertion intact. 1 Publication1
Mutagenesisi101D → A: Drastically reduces palmitoyltransferase activity while leaving expression and membrane insertion intact. 1 Publication1
Mutagenesisi101D → N: Drastically reduces palmitoyltransferase activity while leaving expression and membrane insertion intact. 1 Publication1
Mutagenesisi102S → A: Drastically reduces palmitoyltransferase activity while leaving expression and membrane insertion intact. 1 Publication1
Mutagenesisi113G → A: Mutant with longer amino-acid side chains at position 113 preferentially transfers pentadecane chain (15:0). 1 Publication1
Mutagenesisi113G → C: Mutants with longer amino-acid side chains at position 113 preferentially transfers myristate chain (14:0). 1 Publication1
Mutagenesisi113G → M: Mutants with longer amino-acid side chains at position 113 preferentially transfers laurate chain (12:0). 1 Publication1
Mutagenesisi155S → A: Fully functional. 1 Publication1
Mutagenesisi172Y → A: Does not cause significant structural perturbations of the enzyme, but induces a 2-fold increase in the palmitoyltransferase activity. 1 Publication1
Mutagenesisi172Y → F: Does not cause significant structural perturbations of the enzyme, but induces a 2.3-fold increase in the palmitoyltransferase activity. 1 Publication1

Chemistry databases

DrugBankiDB03967 Dodecyl Sulfate
DB04147 Lauryl Dimethylamine-N-Oxide

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 25UniRule annotationAdd BLAST25
ChainiPRO_000007933226 – 186Lipid A palmitoyltransferase PagPAdd BLAST161

Proteomic databases

PaxDbiP37001
PRIDEiP37001

Expressioni

Inductioni

In magnesium-deficient conditions.1 Publication

Interactioni

Subunit structurei

Homodimer.UniRule annotation3 Publications

Protein-protein interaction databases

BioGridi4260645, 351 interactors
STRINGi316385.ECDH10B_0690

Structurei

Secondary structure

1186
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP37001
SMRiP37001
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP37001

Family & Domainsi

Sequence similaritiesi

Belongs to the lipid A palmitoyltransferase family.UniRule annotationCurated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG41079UR Bacteria
ENOG410XTHE LUCA
HOGENOMiHOG000117945
KOiK12973
OMAiAQTWNEP

Family and domain databases

HAMAPiMF_00837 PagP_transferase, 1 hit
InterProiView protein in InterPro
IPR011250 OMP/PagP_b-brl
IPR009746 Peptid-resist/lipidA_acyl_PagP
PfamiView protein in Pfam
PF07017 PagP, 1 hit
ProDomiView protein in ProDom or Entries sharing at least one domain
PD103779 PagP, 1 hit
SUPFAMiSSF56925 SSF56925, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P37001-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNVSKYVAIF SFVFIQLISV GKVFANADEW MTTFRENIAQ TWQQPEHYDL
60 70 80 90 100
YIPAITWHAR FAYDKEKTDR YNERPWGGGF GLSRWDEKGN WHGLYAMAFK
110 120 130 140 150
DSWNKWEPIA GYGWESTWRP LADENFHLGL GFTAGVTARD NWNYIPLPVL
160 170 180
LPLASVGYGP VTFQMTYIPG TYNNGNVYFA WMRFQF
Length:186
Mass (Da):21,770
Last modified:November 1, 1997 - v2
Checksum:i4BC35B02286844A7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S83396 Genomic DNA Translation: AAN86719.1
D28497 Genomic DNA No translation available.
L29054 Genomic DNA Translation: AAA67555.1
U82598 Genomic DNA Translation: AAB40822.1
U00096 Genomic DNA Translation: AAC73723.1
AP009048 Genomic DNA Translation: BAA35265.2
PIRiD64796
RefSeqiNP_415155.1, NC_000913.3
WP_001103094.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC73723; AAC73723; b0622
BAA35265; BAA35265; BAA35265
GeneIDi946360
KEGGiecj:JW0617
eco:b0622
PATRICifig|1411691.4.peg.1646

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S83396 Genomic DNA Translation: AAN86719.1
D28497 Genomic DNA No translation available.
L29054 Genomic DNA Translation: AAA67555.1
U82598 Genomic DNA Translation: AAB40822.1
U00096 Genomic DNA Translation: AAC73723.1
AP009048 Genomic DNA Translation: BAA35265.2
PIRiD64796
RefSeqiNP_415155.1, NC_000913.3
WP_001103094.1, NZ_LN832404.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1MM4NMR-A26-186[»]
1MM5NMR-A26-186[»]
1THQX-ray1.90A26-186[»]
3GP6X-ray1.40A26-186[»]
ProteinModelPortaliP37001
SMRiP37001
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260645, 351 interactors
STRINGi316385.ECDH10B_0690

Chemistry databases

DrugBankiDB03967 Dodecyl Sulfate
DB04147 Lauryl Dimethylamine-N-Oxide

Proteomic databases

PaxDbiP37001
PRIDEiP37001

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73723; AAC73723; b0622
BAA35265; BAA35265; BAA35265
GeneIDi946360
KEGGiecj:JW0617
eco:b0622
PATRICifig|1411691.4.peg.1646

Organism-specific databases

EchoBASEiEB2097
EcoGeneiEG12180 pagP

Phylogenomic databases

eggNOGiENOG41079UR Bacteria
ENOG410XTHE LUCA
HOGENOMiHOG000117945
KOiK12973
OMAiAQTWNEP

Enzyme and pathway databases

BioCyciEcoCyc:EG12180-MONOMER
MetaCyc:EG12180-MONOMER

Miscellaneous databases

EvolutionaryTraceiP37001
PROiPR:P37001

Family and domain databases

HAMAPiMF_00837 PagP_transferase, 1 hit
InterProiView protein in InterPro
IPR011250 OMP/PagP_b-brl
IPR009746 Peptid-resist/lipidA_acyl_PagP
PfamiView protein in Pfam
PF07017 PagP, 1 hit
ProDomiView protein in ProDom or Entries sharing at least one domain
PD103779 PagP, 1 hit
SUPFAMiSSF56925 SSF56925, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiPAGP_ECOLI
AccessioniPrimary (citable) accession number: P37001
Secondary accession number(s): P77617, Q9R7T4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: November 1, 1997
Last modified: September 12, 2018
This is version 126 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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