EPMC_ECOLI
ID EPMC_ECOLI Reviewed; 182 AA.
AC P76938; P76497;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Elongation factor P hydroxylase;
DE Short=EF-P hydroxylase;
DE EC=1.14.-.-;
DE AltName: Full=EF-P post-translational modification enzyme C;
GN Name=epmC; Synonyms=yfcM; OrderedLocusNames=b2326, JW5381;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION AS EF-P HYDROXYLASE, ACTIVITY REGULATION, GENE NAME, PATHWAY, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12 / AT713, K12 / BW25113, and
RC K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=22706199; DOI=10.1038/nchembio.1001;
RA Peil L., Starosta A.L., Virumae K., Atkinson G.C., Tenson T., Remme J.,
RA Wilson D.N.;
RT "Lys34 of translation elongation factor EF-P is hydroxylated by YfcM.";
RL Nat. Chem. Biol. 8:695-697(2012).
RN [5]
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12 / BW25113, and K12 / MG1655 / ATCC 47076;
RX PubMed=23239623; DOI=10.1126/science.1228985;
RA Ude S., Lassak J., Starosta A.L., Kraxenberger T., Wilson D.N., Jung K.;
RT "Translation elongation factor EF-P alleviates ribosome stalling at
RT polyproline stretches.";
RL Science 339:82-85(2013).
CC -!- FUNCTION: Is involved in the final hydroxylation step of the post-
CC translational modification of translation elongation factor P (EF-P) on
CC 'Lys-34'. Acts after beta-lysylation of 'Lys-34' by EpmA and EpmB. EpmC
CC adds an oxygen atom to the C5 position of 'Lys-34' and does not modify
CC the added beta-lysine. {ECO:0000269|PubMed:22706199}.
CC -!- ACTIVITY REGULATION: Hydroxylation activity is abolished by NADP and
CC increased by NADPH. {ECO:0000269|PubMed:22706199}.
CC -!- DISRUPTION PHENOTYPE: EF-P proteins in the mutant strain displays a
CC modification of +128 Da, whereas a modification of +144 Da is observed
CC in wild-type strains. Cells lack CadA activity (lysine decarboxylase).
CC {ECO:0000269|PubMed:22706199, ECO:0000269|PubMed:23239623}.
CC -!- SIMILARITY: Belongs to the EpmC family. {ECO:0000305}.
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DR EMBL; U00096; AAC75386.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16182.2; -; Genomic_DNA.
DR PIR; D65005; D65005.
DR RefSeq; NP_416829.1; NC_000913.3.
DR RefSeq; WP_001089222.1; NZ_LN832404.1.
DR AlphaFoldDB; P76938; -.
DR SMR; P76938; -.
DR BioGRID; 4260792; 4.
DR BioGRID; 851148; 4.
DR DIP; DIP-11984N; -.
DR IntAct; P76938; 5.
DR STRING; 511145.b2326; -.
DR jPOST; P76938; -.
DR PaxDb; P76938; -.
DR PRIDE; P76938; -.
DR EnsemblBacteria; AAC75386; AAC75386; b2326.
DR EnsemblBacteria; BAA16182; BAA16182; BAA16182.
DR GeneID; 946807; -.
DR KEGG; ecj:JW5381; -.
DR KEGG; eco:b2326; -.
DR PATRIC; fig|511145.12.peg.2422; -.
DR EchoBASE; EB3869; -.
DR eggNOG; COG3101; Bacteria.
DR HOGENOM; CLU_097152_0_0_6; -.
DR OMA; TQSQFEV; -.
DR PhylomeDB; P76938; -.
DR BioCyc; EcoCyc:G7201-MON; -.
DR BioCyc; MetaCyc:G7201-MON; -.
DR PRO; PR:P76938; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IDA:EcoCyc.
DR GO; GO:0004497; F:monooxygenase activity; IDA:UniProtKB.
DR GO; GO:0016709; F: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; IDA:EcoCyc.
DR GO; GO:1901260; P:peptidyl-lysine hydroxylation involved in bacterial-type EF-P lysine modification; IMP:EcoCyc.
DR GO; GO:0043687; P:post-translational protein modification; IDA:UniProtKB.
DR InterPro; IPR007411; EpmC.
DR Pfam; PF04315; EpmC; 1.
PE 1: Evidence at protein level;
KW Monooxygenase; Oxidoreductase; Reference proteome.
FT CHAIN 1..182
FT /note="Elongation factor P hydroxylase"
FT /id="PRO_0000169196"
SQ SEQUENCE 182 AA; 21146 MW; ADD70D0BE3E3198A CRC64;
MNSTHHYEQL IEIFNSCFAD DFNTRLIKGD DEPIYLPADA EVPYNRIVFA HGFYASAIHE
ISHWCIAGKA RRELVDFGYW YCPDGRDAQT QSQFEDVEVK PQALDWLFCV AAGYPFNVSC
DNLEGDFEPD RVVFQRRVHA QVMDYLTNGI PERPARFIKA LQNYYHTPEL TAEQFPWPEA
LN
