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Protein

Lipid A palmitoyltransferase PagP

Gene

pagP

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

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

Enzyme 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

  • lipid A biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

BioCyciEcoCyc:EG12180-MONOMER.
ECOL316407:JW0617-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

  • Cell outer membrane UniRule annotation1 Publication

GO - Cellular componenti

  • cell outer membrane Source: UniProtKB
  • integral component of membrane Source: InterPro
Complete GO annotation...

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

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.
STRINGi511145.b0622.

Structurei

Secondary structure

1186
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi27 – 43Combined sources17
Beta strandi47 – 60Combined sources14
Beta strandi77 – 85Combined sources9
Turni87 – 89Combined sources3
Beta strandi91 – 100Combined sources10
Beta strandi102 – 104Combined sources3
Beta strandi106 – 118Combined sources13
Beta strandi121 – 123Combined sources3
Beta strandi126 – 138Combined sources13
Helixi140 – 142Combined sources3
Beta strandi146 – 158Combined sources13
Beta strandi161 – 168Combined sources8
Beta strandi171 – 174Combined sources4
Beta strandi177 – 186Combined sources10

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...

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.
OMAiKTWRPLA.

Family and domain databases

Gene3Di2.40.160.20. 1 hit.
HAMAPiMF_00837. PagP_transferase. 1 hit.
InterProiIPR011250. OMP/PagP_b-brl.
IPR009746. Peptid-resist/lipidA_acyl_PagP.
[Graphical view]
PfamiPF07017. PagP. 1 hit.
[Graphical view]
ProDomiPD103779. PagP. 1 hit.
[Graphical view] [Entries sharing at least one domain]
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.
PATRICi32116424. VBIEscCol129921_0652.

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.
STRINGi511145.b0622.

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.
PATRICi32116424. VBIEscCol129921_0652.

Organism-specific databases

EchoBASEiEB2097.
EcoGeneiEG12180. pagP.

Phylogenomic databases

eggNOGiENOG41079UR. Bacteria.
ENOG410XTHE. LUCA.
HOGENOMiHOG000117945.
KOiK12973.
OMAiKTWRPLA.

Enzyme and pathway databases

BioCyciEcoCyc:EG12180-MONOMER.
ECOL316407:JW0617-MONOMER.
MetaCyc:EG12180-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP37001.
PROiP37001.

Family and domain databases

Gene3Di2.40.160.20. 1 hit.
HAMAPiMF_00837. PagP_transferase. 1 hit.
InterProiIPR011250. OMP/PagP_b-brl.
IPR009746. Peptid-resist/lipidA_acyl_PagP.
[Graphical view]
PfamiPF07017. PagP. 1 hit.
[Graphical view]
ProDomiPD103779. PagP. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF56925. SSF56925. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPAGP_ECOLI
AccessioniPrimary (citable) accession number: P37001
Secondary accession number(s): P77617, Q9R7T4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: November 1, 1997
Last modified: November 2, 2016
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Overproduction leads to camphor resistance and chromosome condensation.1 Publication

Keywords - Technical termi

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

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.