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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei58 – 581UniRule annotation2 Publications
Sitei67 – 671Role in lipopolysaccharide recognitionUniRule annotation
Active sitei101 – 1011UniRule annotation2 Publications
Active sitei102 – 1021UniRule annotation2 Publications
Sitei172 – 1721Role in the phospholipid gatingUniRule annotation

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi58 – 581H → F: Drastically reduces palmitoyltransferase activity while leaving expression and membrane insertion intact. 1 Publication
Mutagenesisi58 – 581H → N: Drastically reduces palmitoyltransferase activity while leaving expression and membrane insertion intact. 1 Publication
Mutagenesisi101 – 1011D → A: Drastically reduces palmitoyltransferase activity while leaving expression and membrane insertion intact. 1 Publication
Mutagenesisi101 – 1011D → N: Drastically reduces palmitoyltransferase activity while leaving expression and membrane insertion intact. 1 Publication
Mutagenesisi102 – 1021S → A: Drastically reduces palmitoyltransferase activity while leaving expression and membrane insertion intact. 1 Publication
Mutagenesisi113 – 1131G → A: Mutant with longer amino-acid side chains at position 113 preferentially transfers pentadecane chain (15:0). 1 Publication
Mutagenesisi113 – 1131G → C: Mutants with longer amino-acid side chains at position 113 preferentially transfers myristate chain (14:0). 1 Publication
Mutagenesisi113 – 1131G → M: Mutants with longer amino-acid side chains at position 113 preferentially transfers laurate chain (12:0). 1 Publication
Mutagenesisi155 – 1551S → A: Fully functional. 1 Publication
Mutagenesisi172 – 1721Y → A: Does not cause significant structural perturbations of the enzyme, but induces a 2-fold increase in the palmitoyltransferase activity. 1 Publication
Mutagenesisi172 – 1721Y → F: Does not cause significant structural perturbations of the enzyme, but induces a 2.3-fold increase in the palmitoyltransferase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525UniRule annotationAdd
BLAST
Chaini26 – 186161Lipid A palmitoyltransferase PagPPRO_0000079332Add
BLAST

Proteomic databases

PaxDbiP37001.

Expressioni

Inductioni

In magnesium-deficient conditions.1 Publication

Interactioni

Subunit structurei

Homodimer.UniRule annotation3 Publications

Protein-protein interaction databases

BioGridi4260645. 351 interactions.
STRINGi511145.b0622.

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi27 – 4317Combined sources
Beta strandi47 – 6014Combined sources
Beta strandi77 – 859Combined sources
Turni87 – 893Combined sources
Beta strandi91 – 10010Combined sources
Beta strandi102 – 1043Combined sources
Beta strandi106 – 11813Combined sources
Beta strandi121 – 1233Combined sources
Beta strandi126 – 13813Combined sources
Helixi140 – 1423Combined sources
Beta strandi146 – 15813Combined sources
Beta strandi161 – 1688Combined sources
Beta strandi171 – 1744Combined sources
Beta strandi177 – 18610Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MM4NMR-A26-186[»]
1MM5NMR-A26-186[»]
1THQX-ray1.90A26-186[»]
3GP6X-ray1.40A26-186[»]
ProteinModelPortaliP37001.
SMRiP37001. Positions 26-186.
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
EntryMethodResolution (Å)ChainPositionsPDBsum
1MM4NMR-A26-186[»]
1MM5NMR-A26-186[»]
1THQX-ray1.90A26-186[»]
3GP6X-ray1.40A26-186[»]
ProteinModelPortaliP37001.
SMRiP37001. Positions 26-186.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260645. 351 interactions.
STRINGi511145.b0622.

Proteomic databases

PaxDbiP37001.

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: September 7, 2016
This is version 117 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.