(data stored in ACNUC1104 zone)

SWISSPROT: D3VJF7_XENNA

ID   D3VJF7_XENNA            Unreviewed;       325 AA.
AC   D3VJF7;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   16-JAN-2019, entry version 55.
DE   RecName: Full=Elongation factor P--(R)-beta-lysine ligase {ECO:0000256|HAMAP-Rule:MF_00174, ECO:0000256|SAAS:SAAS00675070};
DE            Short=EF-P--(R)-beta-lysine ligase {ECO:0000256|HAMAP-Rule:MF_00174};
DE            EC=6.3.1.- {ECO:0000256|HAMAP-Rule:MF_00174, ECO:0000256|SAAS:SAAS00675046};
DE   AltName: Full=EF-P post-translational modification enzyme A {ECO:0000256|HAMAP-Rule:MF_00174};
DE   AltName: Full=EF-P-lysine lysyltransferase {ECO:0000256|HAMAP-Rule:MF_00174};
GN   Name=poxA {ECO:0000313|EMBL:CBJ88713.1};
GN   Synonyms=epmA {ECO:0000256|HAMAP-Rule:MF_00174};
GN   OrderedLocusNames=XNC1_0642 {ECO:0000313|EMBL:CBJ88713.1};
OS   Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / LMG 1036 /
OS   NCIB 9965 / AN6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406817 {ECO:0000313|EMBL:CBJ88713.1, ECO:0000313|Proteomes:UP000008075};
RN   [1] {ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ88713.1, ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
CC   -!- FUNCTION: With EpmB is involved in the beta-lysylation step of the
CC       post-translational modification of translation elongation factor P
CC       (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine
CC       produced by EpmB, forming a lysyl-adenylate, from which the beta-
CC       lysyl moiety is then transferred to the epsilon-amino group of a
CC       conserved specific lysine residue in EF-P. {ECO:0000256|HAMAP-
CC       Rule:MF_00174}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00174,
CC       ECO:0000256|SAAS:SAAS00682299}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. EpmA subfamily. {ECO:0000256|HAMAP-Rule:MF_00174,
CC       ECO:0000256|SAAS:SAAS00682300}.
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DR   EMBL; FN667742; CBJ88713.1; -; Genomic_DNA.
DR   RefSeq; WP_010848046.1; NC_014228.1.
DR   STRING; 406817.XNC1_0642; -.
DR   EnsemblBacteria; CBJ88713; CBJ88713; XNC1_0642.
DR   KEGG; xne:XNC1_0642; -.
DR   eggNOG; ENOG4105CAP; Bacteria.
DR   eggNOG; COG2269; LUCA.
DR   HOGENOM; HOG000236579; -.
DR   KO; K04568; -.
DR   OMA; EWYRPGF; -.
DR   Proteomes; UP000008075; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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; IEA:InterPro.
DR   GO; GO:0006430; P:lysyl-tRNA aminoacylation; IEA:InterPro.
DR   GO; GO:0071915; P:protein-lysine lysylation; IEA:UniProtKB-UniRule.
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; IPR004525; EpmA.
DR   InterPro; IPR018149; Lys-tRNA-synth_II_C.
DR   Pfam; PF00152; tRNA-synt_2; 1.
DR   PRINTS; PR00982; TRNASYNTHLYS.
DR   TIGRFAMs; TIGR00462; genX; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
DR   PRODOM; D3VJF7.
DR   SWISS-2DPAGE; D3VJF7.
KW   Aminoacyl-tRNA synthetase {ECO:0000313|EMBL:CBJ88713.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00174,
KW   ECO:0000256|SAAS:SAAS00675071};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008075};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00174,
KW   ECO:0000256|SAAS:SAAS00675072};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00174,
KW   ECO:0000256|SAAS:SAAS00675044};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008075}.
FT   DOMAIN       19    321       AA_TRNA_LIGASE_II. {ECO:0000259|PROSITE:
FT                                PS50862}.
FT   NP_BIND     100    102       ATP. {ECO:0000256|HAMAP-Rule:MF_00174}.
FT   NP_BIND     244    245       ATP. {ECO:0000256|HAMAP-Rule:MF_00174}.
FT   REGION       76     78       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00174}.
FT   BINDING     109    109       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00174}.
FT   BINDING     118    118       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00174}.
FT   BINDING     251    251       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00174}.
FT   BINDING     300    300       ATP; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00174}.
SQ   SEQUENCE   325 AA;  36789 MW;  F856C4D64280020F CRC64;
     MNEIANWQPS APIANLLKRA KILAEIRRFF ADRGVLEVET PAMSQATVTD IHLVPFQTRF
     VGPGAADGLT LYLMTSPEYH MKRLLAAGSG SIYQIGKSFR NEEAGRQHNP EFTMLEWYRP
     HYDMYRLMNE VDDLLQQILE CESAESLSYQ QAFIRYLNID PLTASKEKLR EVAAKLDLSN
     IADQEEDRDT LLQLLFVMSV ETQIGIEKPT FVYHFPASQA SLAEISKEDH RVAERFEVYF
     KGMELANGFR ELTDSDEQCL RFEQDNRKRE EMGLPVQPID DHLLAALAHG MPECAGVALG
     VDRLIMLALG ADRMSDVIAF PVGIS
//

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