EPMA_VIBCH
ID EPMA_VIBCH Reviewed; 324 AA.
AC Q9KNS6;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Elongation factor P--(R)-beta-lysine ligase {ECO:0000255|HAMAP-Rule:MF_00174};
DE Short=EF-P--(R)-beta-lysine ligase {ECO:0000255|HAMAP-Rule:MF_00174};
DE EC=6.3.1.- {ECO:0000255|HAMAP-Rule:MF_00174};
DE AltName: Full=EF-P post-translational modification enzyme A {ECO:0000255|HAMAP-Rule:MF_00174};
DE AltName: Full=EF-P-lysine lysyltransferase {ECO:0000255|HAMAP-Rule:MF_00174};
GN Name=epmA {ECO:0000255|HAMAP-Rule:MF_00174}; Synonyms=yjeA;
GN OrderedLocusNames=VC_2655;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
CC -!- FUNCTION: With EpmB is involved in the beta-lysylation step of the
CC post-translational modification of translation elongation factor P (EF-
CC P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced
CC by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is
CC then transferred to the epsilon-amino group of a conserved specific
CC lysine residue in EF-P. {ECO:0000255|HAMAP-Rule:MF_00174}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00174}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC EpmA subfamily. {ECO:0000255|HAMAP-Rule:MF_00174}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF95796.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE003852; AAF95796.1; ALT_INIT; Genomic_DNA.
DR PIR; E82050; E82050.
DR RefSeq; NP_232283.2; NC_002505.1.
DR RefSeq; WP_000185039.1; NZ_LT906614.1.
DR AlphaFoldDB; Q9KNS6; -.
DR SMR; Q9KNS6; -.
DR STRING; 243277.VC_2655; -.
DR DNASU; 2615672; -.
DR EnsemblBacteria; AAF95796; AAF95796; VC_2655.
DR GeneID; 57741252; -.
DR KEGG; vch:VC_2655; -.
DR PATRIC; fig|243277.26.peg.2531; -.
DR eggNOG; COG2269; Bacteria.
DR HOGENOM; CLU_008255_1_1_6; -.
DR OMA; EWYRPGF; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016880; F:acid-ammonia (or amide) ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004824; F:lysine-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR GO; GO:0006430; P:lysyl-tRNA aminoacylation; IBA:GO_Central.
DR GO; GO:0071915; P:protein-lysine lysylation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.930.10; -; 1.
DR HAMAP; MF_00174; EF_P_modif_A; 1.
DR InterPro; IPR004364; Aa-tRNA-synt_II.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004525; EpmA.
DR InterPro; IPR018149; Lys-tRNA-synth_II_C.
DR Pfam; PF00152; tRNA-synt_2; 1.
DR PRINTS; PR00982; TRNASYNTHLYS.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00462; genX; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..324
FT /note="Elongation factor P--(R)-beta-lysine ligase"
FT /id="PRO_0000152730"
FT BINDING 75..77
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00174"
FT BINDING 99..101
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00174"
FT BINDING 108
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00174"
FT BINDING 117
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00174"
FT BINDING 243..244
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00174"
FT BINDING 250
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00174"
FT BINDING 299
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00174"
SQ SEQUENCE 324 AA; 36322 MW; 973F7B70B9AA353C CRC64;
MTNSDWMPTA SISQLKQRAT LLRQIREFFA ERNVLEVETP AMSHATVTDI HLHTFKTEFV
GPGYAKGSAL HLMTSPEFHM KRLLAAGSGC IYQLGKAFRN EENGRYHNPE FTMLEWYRIG
FDHHALMDEM DALLQLVLRC GSAERMTYQE AFLNVLGVCP LEEEMRELKQ VAATLGLSDI
AEPEEDRDTL LQLLFSIGIE PKIGQITPAF VYDFPASQAA LAKINPADPR VADRFEVYFK
GIELANGFHE LDNPAEQLAR FKADNAKRLE MGLTEQPIDY HLIAALEAGL PECAGVALGI
DRLIMLALGE DHIDKVTAFP FPRA
