epmA

Elongation factor P--(R)-beta-lysine ligase

327 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

37.877 kDa

MNKLISWKPRASIHNLFIRAKIINNIRIFFINRGLLEVETPVMSHTTVPDIYLFPFQTNLYFLEKVPEKGVPMYLITSPEYHMKRLLAAGSGPIFQICHSFRNQEYGNYHNPEFTLLEWYRPYYNMVDIMDEVNIFLQTIIHCDSAEMLSYQQVFRLHVGIDPLLAELDELNQVLVKFNLSSTISLYNDRDKLLDFLFLMLVRPHLGNNKPVFIYNFPASQSLLAELNSDDHRVAERFEVYFHGIELANGSRELTDADLQRERFMQENNKQVAMNRPPRLIDEQLLAALECGLPSCSGVALGIDRLLMLTLKAKHISEVMAFSVTDA

epmA

Elongation factor P--(R)-beta-lysine ligase

327 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

37.576 kDa

MSDASLTKINWQPTASIQTLLKRSKIMAEIRQFFTDRGVLEVETPALSEYSVTDVHLSTFSTEFLSPFAKQAKTLHLITSPEYHMKRLLAAGSSSIFQLCRVFRNEESGKRHNPEFTMLEWYRPHFDMYRLINEVDDLLQQILDCEPIESYSYQFVFQTYVGLDPLSASRAQLVEKARKHGFACEEDENRDTLLQFLFSEIVEANIGQERPTTVYHFPSSQAALAQISSEDHRVAERFEIYYKGLELANGFHELNDAKEQIRRFERDNQLREQMNLPPQPLDMRFLAALKAGIPNCSGVALGVDRLIMLALNANHIQEVMAFGVERA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

37.061 kDa

MSETATWQPSASIPNLLKRAAIMTEIRRFFADRGVLEVETPCMSQATVTDIHLFPFETRFVGPGHSQGMNLYLMTSPEYHMKRLLVAGCGPVFQLCRSFRNEEMGRHHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLECQPAESLSYQQVFQRHLEIDPLSADKTQLREAAAKLDLSNIADTEEDRDTLLQLLFTMGVEPHIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYFKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQQPIDNNLLEALKVGMPDCSGVALGVDRLVMLALGAESLAEVIAFTVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.976 kDa

MSETASWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGHSQGMNLWLMTSPEYHMKRLLVAGCGPVFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCPAAESLSYQQAFLRYLEIDPLSADKTQLREVAAKLDLSNVADTEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVIAFSVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.976 kDa

MSETASWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGHSQGMNLWLMTSPEYHMKRLLVAGCGPVFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCPAAESLSYQQAFLRYLEIDPLSADKTQLREVAAKLDLSNVADTEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVIAFSVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.976 kDa

MSETASWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGHSQGMNLWLMTSPEYHMKRLLVAGCGPVFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCPAAESLSYQQAFLRYLEIDPLSADKTQLREVAAKLDLSNVADTEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVIAFSVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.976 kDa

MSETASWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGHSQGMNLWLMTSPEYHMKRLLVAGCGPVFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCPAAESLSYQQAFLRYLEIDPLSADKTQLREVAAKLDLSNVADTEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVIAFSVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.976 kDa

MSETASWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGHSQGMNLWLMTSPEYHMKRLLVAGCGPVFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCPAAESLSYQQAFLRYLEIDPLSADKTQLREVAAKLDLSNVADTEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVIAFSVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.976 kDa

MSETASWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGHSQGMNLWLMTSPEYHMKRLLVAGCGPVFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCPAAESLSYQQAFLRYLEIDPLSADKTQLREVAAKLDLSNVADTEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVIAFSVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.976 kDa

MSETASWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGHSQGMNLWLMTSPEYHMKRLLVAGCGPVFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCPAAESLSYQQAFLRYLEIDPLSADKTQLREVAAKLDLSNVADTEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVIAFSVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.976 kDa

MSETASWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGHSQGMNLWLMTSPEYHMKRLLVAGCGPVFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCPAAESLSYQQAFLRYLEIDPLSADKTQLREVAAKLDLSNVADTEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVIAFSVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.976 kDa

MSETASWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGHSQGMNLWLMTSPEYHMKRLLVAGCGPVFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCPAAESLSYQQAFLRYLEIDPLSADKTQLREVAAKLDLSNVADTEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVIAFSVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.976 kDa

MSETASWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGHSQGMNLWLMTSPEYHMKRLLVAGCGPVFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCPAAESLSYQQAFLRYLEIDPLSADKTQLREVAAKLDLSNVADTEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVIAFSVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.976 kDa

MSETASWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGHSQGMNLWLMTSPEYHMKRLLVAGCGPVFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCPAAESLSYQQAFLRYLEIDPLSADKTQLREVAAKLDLSNVADTEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVIAFSVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.976 kDa

MSETASWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGHSQGMNLWLMTSPEYHMKRLLVAGCGPVFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCPAAESLSYQQAFLRYLEIDPLSADKTQLREVAAKLDLSNVADTEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVIAFSVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.976 kDa

MSETASWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGHSQGMNLWLMTSPEYHMKRLLVAGCGPVFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCPAAESLSYQQAFLRYLEIDPLSADKTQLREVAAKLDLSNVADTEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVIAFSVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.976 kDa

MSETASWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGHSQGMNLWLMTSPEYHMKRLLVAGCGPVFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCPAAESLSYQQAFLRYLEIDPLSADKTQLREVAAKLDLSNVADTEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVIAFSVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.962 kDa

MSETASWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGHSQGMNLWLMTSPEYHMKRLLVAGCGPVFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCPAAESLSYQQAFLRYLEIDPLSADKTQLREVAAKLDLSNVADTEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIDALKVGMPDCSGVALGVDRLVMLALGAETLAEVIAFSVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'. (R)-beta-lysine is 100-fold more efficient as a substrate than either (S)-beta-lysine or L-alpha-lysine. Cannot ligate lysine to any tRNA.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.976 kDa

MSETASWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGHSQGMNLWLMTSPEYHMKRLLVAGCGPVFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCPAAESLSYQQAFLRYLEIDPLSADKTQLREVAAKLDLSNVADTEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVIAFSVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.976 kDa

MSETASWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGHSQGMNLWLMTSPEYHMKRLLVAGCGPVFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCPAAESLSYQQAFLRYLEIDPLSADKTQLREVAAKLDLSNVADTEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVIAFSVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.976 kDa

MSETASWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGHSQGMNLWLMTSPEYHMKRLLVAGCGPVFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCPAAESLSYQQAFLRYLEIDPLSADKTQLREVAAKLDLSNVADTEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVIAFSVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.976 kDa

MSETASWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGHSQGMNLWLMTSPEYHMKRLLVAGCGPVFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCPAAESLSYQQAFLRYLEIDPLSADKTQLREVAAKLDLSNVADTEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVIAFSVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

37.061 kDa

MSETATWQPSASIPNLLKRAAIMTEIRRFFADRGVLEVETPCMSQATVTDIHLFPFETRFVGPGHSQGMNLYLMTSPEYHMKRLLVAGCGPVFQLCRSFRNEEMGRHHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLECQPAESLSYQQVFQRHLEIDPLSADKTQLREAAAKLDLSNIADTEEDRDTLLQLLFTMGVEPHIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYFKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQQPIDNNLLEALKVGMPDCSGVALGVDRLVMLALGAESLAEVIAFTVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.976 kDa

MSETASWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGHSQGMNLWLMTSPEYHMKRLLVAGCGPVFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCPAAESLSYQQAFLRYLEIDPLSADKTQLREVAAKLDLSNVADTEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVIAFSVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.976 kDa

MSETASWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGHSQGMNLWLMTSPEYHMKRLLVAGCGPVFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCPAAESLSYQQAFLRYLEIDPLSADKTQLREVAAKLDLSNVADTEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVIAFSVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.976 kDa

MSETASWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGHSQGMNLWLMTSPEYHMKRLLVAGCGPVFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCPAAESLSYQQAFLRYLEIDPLSADKTQLREVAAKLDLSNVADTEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVIAFSVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.976 kDa

MSETASWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGHSQGMNLWLMTSPEYHMKRLLVAGCGPVFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCPAAESLSYQQAFLRYLEIDPLSADKTQLREVAAKLDLSNVADTEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVIAFSVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.976 kDa

MSETASWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGHSQGMNLWLMTSPEYHMKRLLVAGCGPVFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCPAAESLSYQQAFLRYLEIDPLSADKTQLREVAAKLDLSNVADTEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVIAFSVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.976 kDa

MSETASWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGHSQGMNLWLMTSPEYHMKRLLVAGCGPVFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCPAAESLSYQQAFLRYLEIDPLSADKTQLREVAAKLDLSNVADTEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVIAFSVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.976 kDa

MSETASWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGHSQGMNLWLMTSPEYHMKRLLVAGCGPVFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCPAAESLSYQQAFLRYLEIDPLSADKTQLREVAAKLDLSNVADTEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVIAFSVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.976 kDa

MSETASWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGHSQGMNLWLMTSPEYHMKRLLVAGCGPVFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCPAAESLSYQQAFLRYLEIDPLSADKTQLREVAAKLDLSNVADTEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVIAFSVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.976 kDa

MSETASWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGHSQGMNLWLMTSPEYHMKRLLVAGCGPVFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCPAAESLSYQQAFLRYLEIDPLSADKTQLREVAAKLDLSNVADTEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVIAFSVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.976 kDa

MSETASWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGHSQGMNLWLMTSPEYHMKRLLVAGCGPVFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCPAAESLSYQQAFLRYLEIDPLSADKTQLREVAAKLDLSNVADTEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVIAFSVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.976 kDa

MSETASWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGHSQGMNLWLMTSPEYHMKRLLVAGCGPVFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCPAAESLSYQQAFLRYLEIDPLSADKTQLREVAAKLDLSNVADTEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVIAFSVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.976 kDa

MSETASWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGHSQGMNLWLMTSPEYHMKRLLVAGCGPVFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCPAAESLSYQQAFLRYLEIDPLSADKTQLREVAAKLDLSNVADTEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVIAFSVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.976 kDa

MSETASWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGHSQGMNLWLMTSPEYHMKRLLVAGCGPVFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCPAAESLSYQQAFLRYLEIDPLSADKTQLREVAAKLDLSNVADTEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVIAFSVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.976 kDa

MSETASWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGHSQGMNLWLMTSPEYHMKRLLVAGCGPVFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCPAAESLSYQQAFLRYLEIDPLSADKTQLREVAAKLDLSNVADTEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVIAFSVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.962 kDa

MSETASWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGHSQGMNLWLMTSPEYHMKRLLVAGCGPVFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCPAAESLSYQQAFLRYLEIDPLSADKTQLREVAAKLDLSNVADTEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIDALKVGMPDCSGVALGVDRLVMLALGAETLAEVIAFSVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'. (R)-beta-lysine is 100-fold more efficient as a substrate than either (S)-beta-lysine or L-alpha-lysine. Cannot ligate lysine to any tRNA.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.976 kDa

MSETASWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGHSQGMNLWLMTSPEYHMKRLLVAGCGPVFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCPAAESLSYQQAFLRYLEIDPLSADKTQLREVAAKLDLSNVADTEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVIAFSVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.976 kDa

MSETASWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGHSQGMNLWLMTSPEYHMKRLLVAGCGPVFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCPAAESLSYQQAFLRYLEIDPLSADKTQLREVAAKLDLSNVADTEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVIAFSVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.976 kDa

MSETASWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGHSQGMNLWLMTSPEYHMKRLLVAGCGPVFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCPAAESLSYQQAFLRYLEIDPLSADKTQLREVAAKLDLSNVADTEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVIAFSVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.976 kDa

MSETASWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGHSQGMNLWLMTSPEYHMKRLLVAGCGPVFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCPAAESLSYQQAFLRYLEIDPLSADKTQLREVAAKLDLSNVADTEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVIAFSVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.976 kDa

MSETASWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGHSQGMNLWLMTSPEYHMKRLLVAGCGPVFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCPAAESLSYQQAFLRYLEIDPLSADKTQLREVAAKLDLSNVADTEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVIAFSVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.453 kDa

MSDSASWQPSAPIANLLKRAAIVGQIRRFFSDRGLLEVETPAMSQATVTDIHLVPFQTCFIGPGAAGGMPLYLMTSPEYHMKRLLAAGSGPLFQLCRSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQILDCDSAETLSYQQVFTRHVGIDPLSADKAQLYDAAVKWDLGEAASVEDDRDTLLQLLFAMVVEPNIGHDKPAFVYHFPASQAALAEISTEDHRVADRFEAYFKGIELANGFCELTDAREQRQRFEQDNRKRVAMKLSEQPIDENLLAALAQGMPECSGVALGVDRLVMLALKADRLSDVIAFAVERA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.642 kDa

MSETASWQPSAPIANLLKRAAIMAEIRRFFADRGVLEVETPTMSQATVTDIHLVPFQTRFVGPGAADGLTLYMMTSPEYHMKRLLAAGSGSIYQLGRSFRNEEAGRHHNPEFTMLEWYRPHYDMYRLMDEVEDLLQQILDCDSSERLSYQQAFLRHLDIDPLSADKAQLREAAAKLDLSNIADTEEDRDTLLQLLFTVGVEPHIGRDKPAFVYHFPASQASLAVISTEDHRVAERFEVYFKGIELANGFHELTDGDEQLKRFEQDNRSREKRGLPQHPIDMNLIDALKHGLPDCSGVALGVDRLVMLALGAEKLSDVIAFPVGRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.7 kDa

MSDTASWQPSAPIANLLKRAAIMAEIRRFFADRGVLEVETPTMSQATVTDIHLVPFETRFVGPGAADGLTLYMMTSPEYHMKRLLAAGSGPIYQLGRSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQILDCNSAETLSYQQAFLRHLNIDPLSAEKAQLREVAAKLDLSNIADTEEDRDTLLQLLFTVGVEPYIGRDKPAFIYHFPASQASLAEISTEDHRVAERFEVYFKGIELANGFRELTDGDEQLQRFEQDNRNRAKRGLPQNPIDMNLIAALKQGLPDCSGVALGVDRLVMLALNAERLSDVIAFPVNIA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.7 kDa

MSDTASWQPSAPIANLLKRAAIMAEIRRFFADRGVLEVETPTMSQATVTDIHLVPFETRFVGPGAADGLTLYMMTSPEYHMKRLLAAGSGPIYQLGRSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQILDCNSAETLSYQQAFLRHLNIDPLSAEKAQLREVAAKLDLSNIADTEEDRDTLLQLLFTVGVEPYIGRDKPAFIYHFPASQASLAEISTEDHRVAERFEVYFKGIELANGFRELTDGDEQLQRFEQDNRNRAKRGLPQNPIDMNLIAALKQGLPDCSGVALGVDRLVMLALNAERLSDVIAFPVNIA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.7 kDa

MSDTASWQPSAPIANLLKRAAIMAEIRRFFADRGVLEVETPTMSQATVTDIHLVPFETRFVGPGAADGLTLYMMTSPEYHMKRLLAAGSGPIYQLGRSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQILDCNSAETLSYQQAFLRHLNIDPLSAEKAQLREVAAKLDLSNIADTEEDRDTLLQLLFTVGVEPYIGRDKPAFIYHFPASQASLAEISTEDHRVAERFEVYFKGIELANGFRELTDGDEQLQRFEQDNRNRAKRGLPQNPIDMNLIAALKQGLPDCSGVALGVDRLVMLALNAERLSDVIAFPVNIA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.7 kDa

MSDTASWQPSAPIANLLKRAAIMAEIRRFFADRGVLEVETPTMSQATVTDIHLVPFETRFVGPGAADGLTLYMMTSPEYHMKRLLAAGSGPIYQLGRSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQILDCNSAETLSYQQAFLRHLNIDPLSAEKAQLREVAAKLDLSNIADTEEDRDTLLQLLFTVGVEPYIGRDKPAFIYHFPASQASLAEISTEDHRVAERFEVYFKGIELANGFRELTDGDEQLQRFEQDNRNRAKRGLPQNPIDMNLIAALKQGLPDCSGVALGVDRLVMLALNAERLSDVIAFPVNIA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.7 kDa

MSDTASWQPSAPIANLLKRAAIMAEIRRFFADRGVLEVETPTMSQATVTDIHLVPFETRFVGPGAADGLTLYMMTSPEYHMKRLLAAGSGPIYQLGRSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQILDCNSAETLSYQQAFLRHLNIDPLSAEKAQLREVAAKLDLSNIADTEEDRDTLLQLLFTVGVEPYIGRDKPAFIYHFPASQASLAEISTEDHRVAERFEVYFKGIELANGFRELTDGDEQLQRFEQDNRNRAKRGLPQNPIDMNLIAALKQGLPDCSGVALGVDRLVMLALNAERLSDVIAFPVNIA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.7 kDa

MSDTASWQPSAPIANLLKRAAIMAEIRRFFADRGVLEVETPTMSQATVTDIHLVPFETRFVGPGAADGLTLYMMTSPEYHMKRLLAAGSGPIYQLGRSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQILDCNSAETLSYQQAFLRHLNIDPLSAEKAQLREVAAKLDLSNIADTEEDRDTLLQLLFTVGVEPYIGRDKPAFIYHFPASQASLAEISTEDHRVAERFEVYFKGIELANGFRELTDGDEQLQRFEQDNRNRAKRGLPQNPIDMNLIAALKQGLPDCSGVALGVDRLVMLALNAERLSDVIAFPVNIA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.7 kDa

MSDTASWQPSAPIANLLKRAAIMAEIRRFFADRGVLEVETPTMSQATVTDIHLVPFETRFVGPGAADGLTLYMMTSPEYHMKRLLAAGSGPIYQLGRSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQILDCNSAETLSYQQAFLRHLNIDPLSAEKAQLREVAAKLDLSNIADTEEDRDTLLQLLFTVGVEPYIGRDKPAFIYHFPASQASLAEISTEDHRVAERFEVYFKGIELANGFRELTDGDEQLQRFEQDNRNRAKRGLPQNPIDMNLIAALKQGLPDCSGVALGVDRLVMLALNAERLSDVIAFPVNIA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.7 kDa

MSDTASWQPSAPIANLLKRAAIMAEIRRFFADRGVLEVETPTMSQATVTDIHLVPFETRFVGPGAADGLTLYMMTSPEYHMKRLLAAGSGPIYQLGRSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQILDCNSAETLSYQQAFLRHLNIDPLSAEKAQLREVAAKLDLSNIADTEEDRDTLLQLLFTVGVEPYIGRDKPAFIYHFPASQASLAEISTEDHRVAERFEVYFKGIELANGFRELTDGDEQLQRFEQDNRNRAKRGLPQNPIDMNLIAALKQGLPDCSGVALGVDRLVMLALNAERLSDVIAFPVNIA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.7 kDa

MSDTASWQPSAPIANLLKRAAIMAEIRRFFADRGVLEVETPTMSQATVTDIHLVPFETRFVGPGAADGLTLYMMTSPEYHMKRLLAAGSGPIYQLGRSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQILDCNSAETLSYQQAFLRHLNIDPLSAEKAQLREVAAKLDLSNIADTEEDRDTLLQLLFTVGVEPYIGRDKPAFIYHFPASQASLAEISTEDHRVAERFEVYFKGIELANGFRELTDGDEQLQRFEQDNRNRAKRGLPQNPIDMNLIAALKQGLPDCSGVALGVDRLVMLALNAERLSDVIAFPVNIA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.985 kDa

MSEIADWQPSASIANLLKKAKIVSNIRRFFADRGVLEVETPMMSQATVTDIHLCPFETQFVGPGASQGLKLYLMTSPEYHMKRLLAANSGPIYQMGRCFRNEEAGRYHNPEFTMLEWYRPCFDMYRLMNEVDDLLQEVLDCEASESLSYQQAFLRYLDIDPLSADKEKLREVAAKLDLSNIADTEENRDTLLQLLFVSGVEPHIGLEKPTFIYHFPASQASLAEISSEDHRVAERFEVYFKGVELANGFRELTDAKEQRLRFERDNRQRVAMGLPEQPIDERFLAALEAGLPECSGVALGVDRLIMLALGVERISDVIAFPVYRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.856 kDa

MSETATWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLFPFETRFVGPGHSQGINLYLMTSPEYHMKRLLAAGCGPVFQLCRSFRNEEMGRHHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCQPAESLSYQQAFQRHLEIDPLSADKTQLREAAAKLDLSNIADTEEDRDTLLQLLFTMGVEPHIGKEKPTFIYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQQPIDQNLLDALAAGLPDCSGVALGVDRLVMLALGAESLADVIAFTVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

37.023 kDa

MSETATWQPSASVPNLLKRAAIMTEIRRFFADRGVLEVETPCMSQATVTDIHLFPFETRFVGPGHSQGMNLYLMTSPEYHMKRLLAAGCGPVFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCQPAESLSYQQAFQRHLEIDPLSADKTQLREAAAKLDVSNIADTEEDRDTLLQLLFTVGVEPHIGKEKPTFIYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQQPIDNHLLDALKAGMPDCSGVALGVDRLVMLALGAERLADVIAFTVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.874 kDa

MSETATWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLFPFETRFVGPGHSQGMNLYLMTSPEYHMKRLLAAGCGPVFQLCRSFRNEEMGRHHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCQPAESLSYQQAFQRHLEIDPLSADKTQLREAAAKLDLSNIADTEEDRDTLLQLLFTMGVEPHIGKEKPTFIYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQQPIDQNLLDALAAGLPDCSGVALGVDRLVMLALGAESLADVIAFTVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.87 kDa

MSETATWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLFPFETRFVGPGHSQGINLYLMTSPEYHMKRLLAAGCGPVFQLCRSFRNEEMGRHHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCQPAESLSYQQAFQRHLEIDPLSADKTQLREAAAKLDLSNIADTEEDRDTLLQLLFTMGVEPHIGKEKPTFIYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQQPIDQNLLDALAAGLPDCSGVALGIDRLVMLALGAESLADVIAFTVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.856 kDa

MSETATWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLFPFETRFVGPGHSQGINLYLMTSPEYHMKRLLAAGCGPVFQLCRSFRNEEMGRHHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCQPAESLSYQQAFQRHLEIDPLSADKTQLREAAAKLDLSNIADTEEDRDTLLQLLFTMGVEPHIGKEKPTFIYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQQPIDQNLLDALAAGLPDCSGVALGVDRLVMLALGAESLADVIAFTVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.751 kDa

MSETATWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLFPFETRFVGPGHSQGINLYLMTSPEYHMKRLLAAGCGPVFQLCRSFRNEEMGRHHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCQPAESLSYQQAFQGHLEIDPLSADKTQLREAVAKLDLSNIADTEEDRDTLLQLLLTMGVEPHIGKEKPTFIYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQQPIDQNLLDALAAGLPDCSGVALGVDRLVMLALGAESLADVIAFTVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.856 kDa

MSETATWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLFPFETRFVGPGHSQGINLYLMTSPEYHMKRLLAAGCGPVFQLCRSFRNEEMGRHHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCQPAESLSYQQAFQRHLEIDPLSADKTQLREAAAKLDLSNIADTEEDRDTLLQLLFTMGVEPHIGKEKPTFIYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQQPIDQNLLDALAAGLPDCSGVALGVDRLVMLALGAESLADVIAFTVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.874 kDa

MSETATWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLFPFETRFVGPGHSQGMNLYLMTSPEYHMKRLLAAGCGPVFQLCRSFRNEEMGRHHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCQPAESLSYQQAFQRHLEIDPLSADKTQLREAAAKLDLSNIADTEEDRDTLLQLLFTMGVEPHIGKEKPTFIYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQQPIDQNLLDALAAGLPDCSGVALGVDRLVMLALGAESLADVIAFTVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.904 kDa

MSETATWQPSASIPNLLKRAAIMTEIRRFFADRGVLEVETPCMSQATVTDIHLFPFETRFVGPGHSQGMNLYLMTSPEYHMKRLLAAGCGPVFQLCRSFRNEEMGRHHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCQPAESLSYQQAFQRHLEIDPLSADKTQLREAAAKLDLSNIADTEEDRDTLLQLLFTMGVEPHIGKEKPTFIYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQQPIDQNLLDALAAGLPDCSGVALGVDRLVMLALGAESLADVIAFTVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.874 kDa

MSETATWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLFPFETRFVGPGHSQGMNLYLMTSPEYHMKRLLAAGCGPVFQLCRSFRNEEMGRHHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCQPAESLSYQQAFQRHLEIDPLSADKTQLREAAAKLDLSNIADTEEDRDTLLQLLFTMGVEPHIGKEKPTFIYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQQPIDQNLLDALAAGLPDCSGVALGVDRLVMLALGAESLADVIAFTVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.874 kDa

MSETATWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLFPFETRFVGPGHSQGMNLYLMTSPEYHMKRLLAAGCGPVFQLCRSFRNEEMGRHHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCQPAESLSYQQAFQRHLEIDPLSADKTQLREAAAKLDLSNIADTEEDRDTLLQLLFTMGVEPHIGKEKPTFIYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQQPIDQNLLDALAAGLPDCSGVALGVDRLVMLALGAESLADVIAFTVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.904 kDa

MSETATWQPSASIPNLLKRAAIMTEIRRFFADRGVLEVETPCMSQATVTDIHLFPFETRFVGPGHSQGMNLYLMTSPEYHMKRLLAAGCGPVFQLCRSFRNEEMGRHHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCQPAESLSYQQAFQRHLEIDPLSADKTQLREAAAKLDLSNIADTEEDRDTLLQLLFTMGVEPHIGKEKPTFIYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQQPIDQNLLDALAAGLPDCSGVALGVDRLVMLALGAESLADVIAFTVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.874 kDa

MSETATWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLFPFETRFVGPGHSQGMNLYLMTSPEYHMKRLLAAGCGPVFQLCRSFRNEEMGRHHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCQPAESLSYQQAFQRHLEIDPLSADKTQLREAAAKLDLSNIADTEEDRDTLLQLLFTMGVEPHIGKEKPTFIYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQQPIDQNLLDALAAGLPDCSGVALGVDRLVMLALGAESLADVIAFTVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.841 kDa

MSETATWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLFPFETRFVGPGHSQGINLYLMTSPEYHMKRLLAAGCGPVFQLCRSFRNEEMGRHHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCQPAESLSYQQAFLRHLEIDPLSADKTQLREAAAKLDLSNIADTEEDRDTLLQLLFTMGVEPHIGKEKPTFIYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQQPIDQNLLDALAAGLPDCSGVALGVDRLVMLALGAESLADVIAFTVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34' (Probable). Can also use L-alpha-lysine as a substrate, but probably with lower efficiency. Cannot aminoacylate tRNA(Lys) with lysine.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.856 kDa

MSETATWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLFPFETRFVGPGHSQGINLYLMTSPEYHMKRLLAAGCGPVFQLCRSFRNEEMGRHHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCQPAESLSYQQAFQRHLEIDPLSADKTQLREAAAKLDLSNIADTEEDRDTLLQLLFTMGVEPHIGKEKPTFIYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQQPIDQNLLDALAAGLPDCSGVALGVDRLVMLALGAESLADVIAFTVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.679 kDa

MSETASWQPSAPIANLLKRAAILTEIRRFFADRGVLEVETPTMSQATVTDIHLFPFQTRFVGPGAADGLTLYMMTSPEYHMKRLLAAGSGPIYQMGRSFRNEEAGRHHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCDSAETLSYQQAFLRHLDIDPLSAEKAQLREAAAKLDLSNIADTEEDRDTLLQLLFTVGVEPHIGRDKPAFVYHFPASQASLAEISTEDHRVAERFEVYFKGIELANGFRELTDSREQGQRFAQDNRKRAERGLPQHPIDNNLLDALQHGMPECSGVALGVDRLVMLALGAESLSEVLAFPVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.976 kDa

MSETASWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGHSQGMNLWLMTSPEYHMKRLLVAGCGPVFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCPAAESLSYQQAFLRYLEIDPLSADKTQLREVAAKLDLSNVADTEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVIAFSVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.976 kDa

MSETASWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGHSQGMNLWLMTSPEYHMKRLLVAGCGPVFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCPAAESLSYQQAFLRYLEIDPLSADKTQLREVAAKLDLSNVADTEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVIAFSVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.976 kDa

MSETASWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGHSQGMNLWLMTSPEYHMKRLLVAGCGPVFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCPAAESLSYQQAFLRYLEIDPLSADKTQLREVAAKLDLSNVADTEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVIAFSVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.803 kDa

MSDMASWQPSAPVANLLKRASILSTIRRFFSDRGVLEVDTPSMSQATVTDVHLVPFQTHFVGPGVAQGMMLYLMTSPEYHMKRLLAAGSGPIYQLCRSFRNEESGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLECESAETLSYQQAFIRHLDVDPLSADKTQLREVAAKLDLSNVADNEEDRDTLLQLLFAFGVEPHIGKERPVFVYHFPASQASLAQISTEDHRVAERFEVYYRGVELANGFHELTDAAEQRQRFEQDNRKRAAAGLPQQPIDEHLLAALEHGMPDSSGVALGVDRLIMLALSAERLSEVIAFSVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.862 kDa

MSETATWQPSASIPNLLKRAAIMTEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGHSQGMNLYMMTSPEYHMKRLLAAGCGPVYQLCRSFRNEEMGRHHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCAGAETLSYQQVFQRHLEIDPLSADKTQLREAAAKLDLSNVADTEEDRDTLLQLLFAFGVEPHIGKDRPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFDQDNRKRAARGLPQQPIDTNLLEALKAGLPDSSGVALGVDRLVMLALGAEQLADVIAFTVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.663 kDa

MSDTASWQPSASIANLLKRAAIMAEIRRFFADRGVLEVETPAMSQATVTDVHLFPFQTRFVGPGAAAGIDLYLMTSPEYHMKRLLAAGSGPIYQLCRSFRNEEMGRHHNPEFTMLEWYRPHYDMYRLINEVDDLLQQVLECAPAETLSYQQAFQRHLEIDPLSADKAQLREVAQKLGAGDLANREEDRDTLLQLLFVLGVEPEIGKEKPAFVYHFPATQAALAEISPEDHRVAERFEVYFKGIELANGFRELTDSREQRQRFEQDNRKRAAAGLPQQPIDTYLLDALSAGMPESSGVALGVDRLVMLALKAEQLSDVIAFTVDRC

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

37.06 kDa

MSETATWQPSASIPNLLKRAAIMTEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGHSQGMNLWLMTSPEYHMKRLLVAGCGPIFQLCRSFRNEEMGRHHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCAPAESLSYQQAFQRYLEIDPLSADKAQLREAAAKLDLSNVADEEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQEQRFEQDNRKRAARGLPQHPIDHNLIEALKVGMPDCSGVALGVDRLVMLALGAERLSDVIAFSVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

37.142 kDa

MSEAANWQPSAPISNLLKRADMIKKIRQFFTDRGVLEVDTPCMSQATVTDVHLSTFETRFLAPTMAKSLSLYMTTSPEYHMKRLLAAGSGPIYQMGRCFRNEEMGRYHNPEFTLLEWYRPHYDMYRLMDEVDDLLQQILTCHSAETLSYQQAFLRHLNIDPLSADETQIKEAAVRLNLASITDNEKDRDTFLQLLFMAGVEPYIGRDKPVFIYHFPASQAALASISTEDYRVAERFEVYFKGIELANGFYELTDSAEQQQRFEQDNRQRAALGLPKRSIDERFIAALKHGLPPCSGVALGIDRLVMLSVNAENLSEVMAFPVERA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.881 kDa

MSETATWQPSAPIPNLLKRAAVMAEIRRFFTDRGVLEVETPCMSQATVTDIHLFPFETRFVGPGHSQGLNLYLMTSPEYHMKRLLAAGCGPVFQLCRSFRNEEMGRHHNPEFTMLEWYRPCYDMYRLINEVDDLLQQVLECQPAESLSYQQAFQRHLDIDPLSADKTQLREVAAKLDLSNIADTEEDRDTLLQLLFTMGVEPHIGKDRPTFIYHFPATQASLAQISPEDHRVAERFEVYYKGIELANGFHELTDAREQRLRFEQDNRKRAARGLPQQPIDNNLLAALEAGLPDCSGVALGVDRVVMLALGAESIGEVIAFTVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.846 kDa

MSETATWQPSAPIPNLLKRAAVMAEIRRFFTDRGVLEVETPCMSQATVTDIHLFPFETRFVGPGHSQGLNLYLMTSPEYHMKRLLAAGCGPVFQLCRSFRNEEMGRHHNPEFTMLEWYRPCYDMYRLINEVDDLLQQVLECQPAESLSYQQAFQRHLEIDPLSADKAQLREVAAKLDLSNIADTEEDRDTLLQLLFTMGVEPHIGKDRPTFIYHFPATQASLAQISPEDHRVAERFEVYYKGIELANGFHELTDAHEQRLRFEQDNRKRAARGLPQQPIDNNLLAALEAGLPDCSGVALGVDRVVMLALGAESIGEVIAFTVDRA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.782 kDa

MSETTSWQPSASVANLLKRASIVAAVRRFFTDRGVLEVETPAMSQATVTDVFLYPFQTRFVGPGAADGMTLYLMTSPEYHMKRLLAAGSGPIFQLCRSFRNEESGRHHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCESAEMLSYQQAFLRHLEIDPLSVDKAQLREAAEKLGLGDIACREDDRDSLVQMLFTFGVEPNIGRDKPAFVYHFPATQASLAEISSEDHRVAERFEVYFKGIELANGFRELTDADEQRQRFEQDNRKRAARGLSQQPIDENLLAALKNGLPECSGVALGVDRLIMLALKAEKLSDVIAFSVERA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.926 kDa

MSETTSWQPSASVANLLKRASIIAAIRRFFTDRGVLEVETPAMSQATVTDIFLYPFQTRFVGPGAADGMTMYLMTSPEYHMKRLLAAGSGPIFQLCRSFRNEESGRHHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCESAEMLSYQQAFLRHLELDPLSVDKAQLREAAEKLGLGDIACREDDRDSLVQMLFTFGVEPHIGRDKPAFVYHFPATQASLAEISSEDHRVAERFEVYFKGIELANGFRELTDADEQRQRFEQDNRKRAARDLPQQPIDENLLAALKHGLPECAGVALGVDRLIMLALNAEKLSDVIAFSVERA

epmA

Elongation factor P--(R)-beta-lysine ligase

325 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.754 kDa

MSETANWQPSAAIANLLKRATILAEIRRFFADRGVLEVETPAMGQFTVTDIQLFSFQTEFVGPGAADGMTLYLMTSPEYHMKRLLAAGSGPIYQLGRCFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQILDCESAESLSYQQAFLRYLDIDPLSAEKEKLREIAAKLDLSNIADIEEDRDTLLQLLFAVGVEPHIGTEKPTFIYHFPASQASLAEISKEDHRVAERFEVYFKGVELANGFRELTDSHEQCQRFERDNRKRAALGLPVRPIDENLIGALKQGMPECAGVALGVDRLVMLALGAEKLSDVMAFSITKA

epmA

Elongation factor P--(R)-beta-lysine ligase

324 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.322 kDa

MTNSDWMPTASISQLKQRATLLRQIREFFAERNVLEVETPAMSHATVTDIHLHTFKTEFVGPGYAKGSALHLMTSPEFHMKRLLAAGSGCIYQLGKAFRNEENGRYHNPEFTMLEWYRIGFDHHALMDEMDALLQLVLRCGSAERMTYQEAFLNVLGVCPLEEEMRELKQVAATLGLSDIAEPEEDRDTLLQLLFSIGIEPKIGQITPAFVYDFPASQAALAKINPADPRVADRFEVYFKGIELANGFHELDNPAEQLARFKADNAKRLEMGLTEQPIDYHLIAALEAGLPECAGVALGIDRLIMLALGEDHIDKVTAFPFPRA

epmA

Elongation factor P--(R)-beta-lysine ligase

324 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

37.88 kDa

MKKKIWKSSASIEDLIKRSNIISNIRLFFSKKNILEVETPILSRSTVTDVHLTSFETNYISSDNIDELKLWLTTSPEYHMKRLLASESGSIYQICHSFRNKELGRYHNPEFTMLEWYQPFCSMKKFIKEIDIFLQIILKCNKSDKVSYQDLFIDFLKIDPLCANLLELHQISKKLKLDHLTHSENNLNKLIQLLFTLKIEPNIGKEKPLFVYHFPAEQASLAAINLKDPRISERFEIFFKGIELGNGFYELIDVNEQKKRFIRDNKERRSMNLPIRKIDNFFLSALSYGLPPCSGVAIGLDRLIMLILNKKSIHEVIAFPVDRC

epmA

Elongation factor P--(R)-beta-lysine ligase

324 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

37.898 kDa

MKKKIWKSSASIEDLIKRSNIISNIRLFFSKKNILEVETPILSRSTVTDVHLTSFETNYISSDNIDELKLWLTTSPEYHMKRLLASESGSIYQICHSFRNKEIGRYHNPEFTMLEWYQPFCSMKKFIKEIDIFLQIILKCNKSDKVSYQDLFIDFLKIDPLCTNLLELHQISKKLKLDHLTHSENNLNKLIQLLFTLKIEPNIGKEKPLFVYHFPAEQASLAAINLKDPRISERFEIFFKGIELGNGFYELIDVNEQKKRFIRDNKERRSMNLPTRKIDNFFLSALSYGLPPCSGVAIGLDRLIMLILNKKSIHEVIAFPVDRC

epmA

Elongation factor P--(R)-beta-lysine ligase

324 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

38.308 kDa

MKKKWKPSASIKDLMKRSKIIADIRSFFLKKNIMEVETPILSQSGVTDVNLMPFITNYFSFNDNIKKKNLWLITSPEYHMKRLLSAGSGSIYQICRSFRNQEFGQYHNPEFTMLEWYQLSCSMEKMIEEIDFFFQKILNFNKADKISYQEVFMKFLKIDPLSTSLSELFQCYKKFNLKNLIYLENDLNQLIENIFTLQIQPFLGKEKPLFVYHFPSEQACLASINKKDSRVSERFEIFFKGIELGNGFHELTDYFEQRKRFIKDNRKRCDMNLPEQKIDDYFLDAIHHGLPTCSGVAIGLDRLIMIALNKNSIDQVMSFSFERS

epmA

Elongation factor P--(R)-beta-lysine ligase

324 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

37.88 kDa

MKKKIWKSSASIEDLIKRSNIISNIRLFFSKKNILEVETPILSRSTVTDVHLTSFETNYISSDNIDELKLWLTTSPEYHMKRLLASESGSIYQICHSFRNKELGRYHNPEFTMLEWYQPFCSMKKFIKEIDIFLQIILKCNKSDKVSYQDLFIDFLKIDPLCANLLELHQISKKLKLDHLTHSENNLNKLIQLLFTLKIEPNIGKEKPLFVYHFPAEQASLAAINLKDPRISERFEIFFKGIELGNGFYELIDVNEQKKRFIRDNKERRSMNLPIRKIDNFFLSALSYGLPPCSGVAIGLDRLIMLILNKKSIHEVIAFPVDRC

epmA

Elongation factor P--(R)-beta-lysine ligase

324 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.295 kDa

MSVNLWAPSASIATLKQRAVILRSIREFFYARNVMEVETPSLSGASVTDIHLVSFNTRFVGPGHASGLELYLQTSPEFAMKRLLAAGSGPIFQLCKAFRNEEAGSHHNPEFTMLEWYRPGFDEFALMAEIDELMQLILDVAPSERLTYQHAFEQVLGLDPLTASLEQLQQLACEQGFADIAKNETHRDTLLQLLFCMKVEPTIGQHKPCFVYHFPASQAALAQICDHDSRVAGRFELYYKNMELANGFNELTNATEQAKRFNDDNEYRKQNGLKQVPMDKHLIAALEHGLAPCAGVALGIDRLVMLATQKSNIKEVIAFDVTRA

epmA

Elongation factor P--(R)-beta-lysine ligase

323 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.197 kDa

MQTTWQPTASMEQLRQRAALITAIRQFFAERQVMEVDTPAMSHATVTDIHLHTFQTEFVGPGYADGSKLFFMTSPEFHMKRLLAAGSGCIYQINKAFRNEENGRHHNPEFTMLEWYRIGFDHHKLMDEMDDLLQLVLKCGAAERMTYQQAFIDVLGVCPLEGSMQELKVVAAKLGLSDIAEPEEDRDTLLQLLSSIGVEAKIGQQVPAFVYDFPASQAALAKINPQDIRVADRFEVYFKGIELANGFHELDNPKEQLARFEQDNAKRLDMGLKPQPIDYHLIGALEAGLPDCAGVALGVDRLIMLALGCDHIDQVTAFPFPIA

epmA

Elongation factor P--(R)-beta-lysine ligase

323 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.294 kDa

MQTNWQPTASIEQLRQRATLIAAIRQFFAERQVMEVDTPAMSHATVTDIHLHTFQTEFVGPGYADGSKLFFMTSPEFHMKRLLAAGSGCIYQINKAFRNEENGRYHNPEFTMLEWYRVGFDHHKLMDEMDDLLQLVLKCGAAQRMTYQQAFIDVLGVCPLEGSMTELKAAASKLGLSDIAEPEEDRDTLLQLLFSVGVENKIGQDVPAFVYDFPASQAALAKINPQDHRVADRFEVYFKGIELANGFHELDNPKEQLARFEQDNAKRIEMGLKPQPIDYHLISALEAGLPDCAGVALGIDRLIMLALGCDHIDQVTAFPFPIA

epmA

Elongation factor P--(R)-beta-lysine ligase

323 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.556 kDa

MHSTWQPAATIKQLKQRADILNQIRQFFVERNVMEVDTPAMSHATVTDVHLHTFKTEFVGPGYAHGQPLFFMTSPEFHMKRLLAAGSGCIYQICKSFRNEENGRYHNPEFTMLEWYRVGFDHHDLMDEMDLLLQQVLKSGTAERMTYQQAFIDVLGVCPLEDSMDTLKQAAAKLGLSDIADPEQDRDTLLQLLFSIGVEAKIGQQVPAFVYDFPASQAALAKINPNDSRVADRFEVYFKGIELANGFHELDKPQEQLKRFEDDNTKRIEMGLSPQPIDHHLIEALKAGLPDCAGVALGIDRLIMLALGYDHIDDVTAFPFPRS

epmA

Elongation factor P--(R)-beta-lysine ligase

323 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.147 kDa

MQADWKPTASIEQLRQRAVLIANIRQFFAQRGVLEVDTPAMSHATVTDIHLHTFQTEFVGPGYAQGRHLHLMTSPEFHMKRLLAAGSGCIYQMAKAFRNEENGRHHNPEFTMLEWYRVGFDHHQLMDEMDDLLQLILKCGTAERMTYQQAFLTVLGVCPLEGSMAELKSVAARLGLSDIAEPEEDRDTLLQLLFSIGVEAKIGQQVPAFVYDFPASQAALAKINPNDPRVADRFEVYFKGIELANGFHELDNPQEQLTRFEQDNAKRIDMGLTPQPIDYHLIAALESGLPACAGVALGVDRLIMLSLGCTHIDEITAFPFPIA

epmA

Elongation factor P--(R)-beta-lysine ligase

323 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.147 kDa

MQADWKPTASIEQLRQRAVLIANIRQFFAQRGVLEVDTPAMSHATVTDIHLHTFQTEFVGPGYAQGRHLHLMTSPEFHMKRLLAAGSGCIYQMAKAFRNEENGRHHNPEFTMLEWYRVGFDHHQLMDEMDDLLQLILKCGTAERMTYQQAFLTVLGVCPLEGSMAELKSVAARLGLSDIAEPEEDRDTLLQLLFSIGVEAKIGQQVPAFVYDFPASQAALAKINPNDPRVADRFEVYFKGIELANGFHELDNPQEQLTRFEQDNAKRIDMGLTPQPIDYHLIAALESGLPACAGVALGVDRLIMLSLGCTHIDEITAFPFPIA

epmA

Elongation factor P--(R)-beta-lysine ligase

323 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

37.302 kDa

MFEQEQWQPTANVETLFARAKIINNIRRFFTDRGVLEVETPILSEFGVTDVHLSTFSTEFVAPQAERSKTLWLNTSPEYHMKRLLAAGTGAIFQLCHVFRNEEAGSRHNPEFTMLEWYRPHFDMYRLINEVDDLLQQILDCEPAESMSYQFAFQEFVGVDPLSAERPILVELARKYNFMCDLDEDRDTLLQFLFSTVVEPKIGQERPVAVYHFPATQAALAQISSEDHRVAERFEFYYKGLELANGFHELTDHREQLHRFEQDNVQRAKLALPQREIDRRLLGALQAGVPNTSGVALGVDRLVMIALDKKRIEEVMAFAINNA

epmA

Elongation factor P--(R)-beta-lysine ligase

323 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

37.165 kDa

MTALNHWQPSADIKNLLKRAKIIAEIRQFFTERGLLEVETPVLSEFGVTDLHLSTFSTEFLAPFGEQSKTLWLSTSPEYHMKRLLAAGSGPIFQISKVFRNEEAGNRHNPEFTMLEWYRPHFHMHRLINEVDDLLQQILDCPPAESLSYQFVFQEYVGLDPLSAERSELIEAARKHNFMAEDNEDRDTLLQFLFSEVVEPQIGKERPIAVYHFPSTQAALAQVSPEDQRVAERFEFYYKGLELANGFHELADAQEQRHRFELDNQQRQKCELPTREIDERFLAALEAGMPDASGVALGIDRLMMIALDCEKINDVISFAMDNA

epmA

Elongation factor P--(R)-beta-lysine ligase

323 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

37.133 kDa

MTALNHWQPSADIKNLLKRAKIIAEIRQFFTERGLLEVETPVLSEFGVTDLHLSTFSTEFLAPFGEQSKTLWLSTSPEYHMKRLLAAGSGPIFQISKVFRNEEAGNRHNPEFTMLEWYRPHFHMHRLINEVDDLLQQILDCPPAESLSYQFVFQEYVGLDPLSAERSELIEAARKHNFMAEDNEDRDTLLQFLFSEVVEPQIGKERPIAVYHFPSTQAALAQVSPEDQRVAERFEFYYKGLELANGFHELADAQEQRHRFELDNQQRQKCELPTREIDERFLAALEAGMPDASGVALGIDRLMMIALDCEKINDVISFAVDNA

epmA

Elongation factor P--(R)-beta-lysine ligase

323 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

37.156 kDa

MTALNHWQPSADIKNHLKRAKIIAKIRQFFTERGLLEVETPVLSEFGVTDLHLSTFSTEFLAPFGEQSKTLWLSTSPEYHMKRLLAAGSGPIFQISKVFRNEEAGNRHNPEFTMLEWYRPHFHMHRLINEVDDLLQQILDCPPAESLSYQFVFQEYVGLDPLSAERSELIEAARKHNFMAEDNEDRDTLLQFLFSEVVEPQIGKERPIAVYHFPSTQAALAQVSPEDQRVAERFEFYYKGLELANGFHELADAQEQRHRFELDNQQRQKCELPTREIDERFLAALEAGMPDASGVALGIDRLMMIALDCEKINDVISFAVDNA

epmA

Elongation factor P--(R)-beta-lysine ligase

323 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.724 kDa

MSLNEQWQPSASIQNLLARAKIIADIRRFFTERGLLEVETPVLSEFGVTDVHLSTFSTAFTSPFMEKSKTLWLTTSPEYHMKRLLAAGSGAIFQLCKVFRNEESGKKHNPEFTMLEWYRPHFDMHRLINEVDDLLQQTLDCEPAEMASYQFVFQEHVGIDPLSAPINELIEKARECHLDGAENEDRDTLLQFLFSTLVEPNIGQNKPIAVYHFPATQAALAQISSEDHRVAERFEFYYKGIELANGFNELTDAQEQEHRFNQDNRLREQLGLPQHEIDHRFLGALQAGLPNTAGVALGVDRLIMLALGAENISEVISFNIDCA

epmA

Elongation factor P--(R)-beta-lysine ligase

323 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.724 kDa

MSLNEQWQPSASIQNLLARAKIIADIRRFFTERGLLEVETPVLSEFGVTDVHLSTFSTAFTSPFMEKSKTLWLTTSPEYHMKRLLAAGSGAIFQLCKVFRNEESGKKHNPEFTMLEWYRPHFDMHRLINEVDDLLQQTLDCEPAEMASYQFVFQEHVGIDPLSAPINELIEKARECHLDGAENEDRDTLLQFLFSTLVEPNIGQNKPIAVYHFPATQAALAQISSEDHRVAERFEFYYKGIELANGFNELTDAQEQEHRFNQDNRLREQLGLPQHEIDHRFLGALQAGLPNTAGVALGVDRLIMLALGAENISEVISFNIDCA

epmA

Elongation factor P--(R)-beta-lysine ligase

323 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

37.075 kDa

MFEQEAWQPSAPIKTLFTRAKIIREIRKFFTERGLLEVETPVLSEFGVTDVHLSTFNTEFIAPIGENSKTLWLMTSPEYHMKRLLAAGSGAIFQICRVFRNEEAGSRHNPEFTMLEWYRPHFDMYRLINEVDDLLQQILDCEPAESFSYQFVFQQYVGLDPLSAPRAELVAKAREHHFMCDENEERDTLLEFLFSTVVEPQIGQTRPAVIYHFPASQAALAQISSEDHRVAERFEFYFKGLELANGFNELTDANEQLIRFERDNRQREKMGLPQRAIDKRLLAALEAGMPNCAGVALGVDRLLMAALNANRIEEVMAFGVNNA

epmA

Elongation factor P--(R)-beta-lysine ligase

323 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.859 kDa

MFEQENWQPSASIENLLARAKIIAEIRRFFTDRGLLEVETPVLSEFGVTDVHLSTFNTTFISPTAEKSKALWLSTSPEYHMKRLLAAGSGPIFQLCHVFRNEEAGQRHNPEFTMLEWYRPHFDMYRLINEVDDLLQQILDCKPTESLSYQFVFQEYVGLDPLSAEKAELVAKAKQYHLQQAEQEDRDTLLQFLFSTVVEPNIGKENPVAVYHFPATQAALAQISSEDHRVAERFEFYYKGLELANGFHELTDVNEQLHRFEQDNVQRQKMGLPQRQIDKRLLGALQAGVPNCSGIALGVDRLLMIALGANAIHEVMAFGIENA

epmA

Elongation factor P--(R)-beta-lysine ligase

323 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.357 kDa

MSQPWQPTASIKQLKQRAAVLSSIRDFFAGKEVIEVDTPAMSQATVTDVHLHTFQTEFVGPGYAGGQTLYMMTSPEFHMKRLLSAGSGPIYQICKSFRNEESGRYHNPEFTMLEWYRPDFDHHDLMNEMDELLQLVLQCDKAERMSYQQAFIQELGVCPLEGTMEQLKGVARTLGLADIADPEQDRDTLLQLLFSMGVENKIGQQVPAFVYDFPASQAALAQINPTDNRVAERFEVYFKGIELANGFHELANGDEQLVRFEQDNMKRISMGLKPQPIDLHLIEALRAGFPDCAGVALGIDRLIMLALKLDHIDQVTAFPIDIA

epmA

Elongation factor P--(R)-beta-lysine ligase

322 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

36.924 kDa

MSEHQWKPTASIQTLLSRAKIIAEIRQFFSERGLLEVETPILSEFGVTDVHLSTFSTKLISPFQKKEKTLWLSTSPEYPMKRLLSAGSGAIFQLCKVFRNEEAGKKHSPEFTMLEWYRPYFDMYRLINEVDDLLQYILDCEPAESMSYQFAFQEYVGIDPLSASQDKLIEKAKEYCLENAEREDRDTLLQFLFNVAVESQIGKDKPVAIYHFPATQAALAQISSEDHRVAERFEFYYKGLELANGFCELTDANEQRHRFEQDNKQRERLGLPIHQIDERFLAALKAGVPNCSGVALGVDRLIMIALGLENINEVIAFSIENA

epmA

Elongation factor P--(R)-beta-lysine ligase

322 amino acids

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P.

Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

37.911 kDa

MNCNYLWKSSALLKNLHRRAKIIFEIRNYFFNLGILEVETPILSNYSVTDVNFIPFKTKLQITKKRMWLVPSPEYHMKRLLVQNIGAIYQISRSFRNNEFGGPYHNPEFTMLEWYSPYCNMFDFMKKVEKFLVFCLKVVQVKYISYQRAFIKYLNIDPLLAKKRELLDLINKFKFNHLISDCDSISTLLEILFTLKIEPNLNNKKLIFVYHYPADQAILAAINDNDSRVSDRFEVFFKGVELGNGFYELTDQAEHIRRFKLNNIQRRHKGICSVEVDQFFLKSLSRGLPPCSGIAIGLDRLIMLSLNLKTINEVIAFPIERC