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Protein

Elongation factor P hydroxylase

Gene

epmC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Is involved in the final hydroxylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Acts after beta-lysylation of 'Lys-34' by EpmA and EpmB. EpmC adds an oxygen atom to the C5 position of 'Lys-34' and does not modify the added beta-lysine.1 Publication

Enzyme regulationi

Hydroxylation activity is abolished by NADP and increased by NADPH.1 Publication

GO - Molecular functioni

  • metal ion binding Source: EcoCyc
  • monooxygenase activity Source: UniProtKB
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen Source: EcoCyc

GO - Biological processi

  • peptidyl-lysine hydroxylation involved in bacterial-type EF-P lysine modification Source: EcoCyc
  • post-translational protein modification Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Enzyme and pathway databases

BioCyciEcoCyc:G7201-MONOMER.
ECOL316407:JW5381-MONOMER.
MetaCyc:G7201-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation factor P hydroxylase (EC:1.14.-.-)
Short name:
EF-P hydroxylase
Alternative name(s):
EF-P post-translational modification enzyme C
Gene namesi
Name:epmC
Synonyms:yfcM
Ordered Locus Names:b2326, JW5381
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG14116. epmC.

Pathology & Biotechi

Disruption phenotypei

EF-P proteins in the mutant strain displays a modification of +128 Da, whereas a modification of +144 Da is observed in wild-type strains. Cells lack CadA activity (lysine decarboxylase).2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001691961 – 182Elongation factor P hydroxylaseAdd BLAST182

Proteomic databases

PaxDbiP76938.
PRIDEiP76938.

Interactioni

Protein-protein interaction databases

BioGridi4260792. 4 interactors.
DIPiDIP-11984N.
IntActiP76938. 5 interactors.
STRINGi511145.b2326.

Structurei

3D structure databases

ProteinModelPortaliP76938.
SMRiP76938.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the EpmC family.Curated

Phylogenomic databases

eggNOGiENOG4108BPE. Bacteria.
COG3101. LUCA.
HOGENOMiHOG000122499.
KOiK09906.
OMAiHAQVMQY.

Family and domain databases

InterProiIPR007411. EpmC.
[Graphical view]
PfamiPF04315. EpmC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P76938-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNSTHHYEQL IEIFNSCFAD DFNTRLIKGD DEPIYLPADA EVPYNRIVFA
60 70 80 90 100
HGFYASAIHE ISHWCIAGKA RRELVDFGYW YCPDGRDAQT QSQFEDVEVK
110 120 130 140 150
PQALDWLFCV AAGYPFNVSC DNLEGDFEPD RVVFQRRVHA QVMDYLTNGI
160 170 180
PERPARFIKA LQNYYHTPEL TAEQFPWPEA LN
Length:182
Mass (Da):21,146
Last modified:July 15, 1999 - v2
Checksum:iADD70D0BE3E3198A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC75386.1.
AP009048 Genomic DNA. Translation: BAA16182.2.
PIRiD65005.
RefSeqiNP_416829.1. NC_000913.3.
WP_001089222.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75386; AAC75386; b2326.
BAA16182; BAA16182; BAA16182.
GeneIDi946807.
KEGGiecj:JW5381.
eco:b2326.
PATRICi32120025. VBIEscCol129921_2422.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC75386.1.
AP009048 Genomic DNA. Translation: BAA16182.2.
PIRiD65005.
RefSeqiNP_416829.1. NC_000913.3.
WP_001089222.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP76938.
SMRiP76938.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260792. 4 interactors.
DIPiDIP-11984N.
IntActiP76938. 5 interactors.
STRINGi511145.b2326.

Proteomic databases

PaxDbiP76938.
PRIDEiP76938.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75386; AAC75386; b2326.
BAA16182; BAA16182; BAA16182.
GeneIDi946807.
KEGGiecj:JW5381.
eco:b2326.
PATRICi32120025. VBIEscCol129921_2422.

Organism-specific databases

EchoBASEiEB3869.
EcoGeneiEG14116. epmC.

Phylogenomic databases

eggNOGiENOG4108BPE. Bacteria.
COG3101. LUCA.
HOGENOMiHOG000122499.
KOiK09906.
OMAiHAQVMQY.

Enzyme and pathway databases

BioCyciEcoCyc:G7201-MONOMER.
ECOL316407:JW5381-MONOMER.
MetaCyc:G7201-MONOMER.

Miscellaneous databases

PROiP76938.

Family and domain databases

InterProiIPR007411. EpmC.
[Graphical view]
PfamiPF04315. EpmC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiEPMC_ECOLI
AccessioniPrimary (citable) accession number: P76938
Secondary accession number(s): P76497
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: July 15, 1999
Last modified: November 2, 2016
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. 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.