ID   EPMC_HAEIN              Reviewed;         178 AA.
AC   P44255;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 93.
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; OrderedLocusNames=HI_1563;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the EpmC family. {ECO:0000305}.
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DR   EMBL; L42023; AAC23212.1; -; Genomic_DNA.
DR   PIR; D64036; D64036.
DR   RefSeq; NP_439712.1; NC_000907.1.
DR   RefSeq; WP_005688501.1; NC_000907.1.
DR   AlphaFoldDB; P44255; -.
DR   SMR; P44255; -.
DR   STRING; 71421.HI_1563; -.
DR   EnsemblBacteria; AAC23212; AAC23212; HI_1563.
DR   KEGG; hin:HI_1563; -.
DR   PATRIC; fig|71421.8.peg.1634; -.
DR   eggNOG; COG3101; Bacteria.
DR   HOGENOM; CLU_097152_0_0_6; -.
DR   OMA; TQSQFEV; -.
DR   PhylomeDB; P44255; -.
DR   BioCyc; HINF71421:G1GJ1-1582-MON; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR007411; EpmC.
DR   Pfam; PF04315; EpmC; 1.
PE   3: Inferred from homology;
KW   Monooxygenase; Oxidoreductase; Reference proteome.
FT   CHAIN           1..178
FT                   /note="Elongation factor P hydroxylase"
FT                   /id="PRO_0000169197"
SQ   SEQUENCE   178 AA;  20604 MW;  BD3BF8F231D2B638 CRC64;
     MEHKLEDIIA IFNQCFEEEY NTRLVKGGDE PIYLPANDEV PYNAIYFARG FYSSALHEIA
     HWLVAGKERR KLEDFGYWYE PDGRSEERQR DFEKVEVKPQ ALEWILATAA GFRYFASADN
     LNGNPGDTQP FKQAVYEQVK IYAEKGLPKR AETLRKALVA FYSTEDDINL AKFDVTCI