| Tag | Content |
|---|
| CPLM ID | CPLM-018437 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase |
Protein Synonyms/Alias | Meso-A2pm-adding enzyme; Meso-diaminopimelate-adding enzyme; UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase; UDP-MurNAc-tripeptide synthetase; UDP-N-acetylmuramyl-tripeptide synthetase |
Gene Name | murE |
Gene Synonyms/Alias | STM0123 |
Created Date | July 27, 2013 |
Organism | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
NCBI Taxa ID | 99287 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 456 | TNAIMQAKDNDVVLI | acetylation | [1] |
|
Reference | [1] Regulation of cellular metabolism by protein lysine acetylation. Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL. Science. 2010 Feb 19;327(5968):1000-4. [ PMID: 20167786] |
Functional Description | Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan (By similarity). |
Sequence Annotation | NP_BIND 116 122 ATP (Potential).
REGION 44 46 UDP-MurNAc-L-Ala-D-Glu binding (By
REGION 158 159 UDP-MurNAc-L-Ala-D-Glu binding (By
REGION 414 417 Meso-diaminopimelate binding (By
MOTIF 414 417 Meso-diaminopimelate recognition motif.
BINDING 27 27 UDP-MurNAc-L-Ala-D-Glu; via carbonyl
BINDING 29 29 UDP-MurNAc-L-Ala-D-Glu (By similarity).
BINDING 157 157 UDP-MurNAc-L-Ala-D-Glu (By similarity).
BINDING 185 185 UDP-MurNAc-L-Ala-D-Glu (By similarity).
BINDING 191 191 UDP-MurNAc-L-Ala-D-Glu (By similarity).
BINDING 193 193 UDP-MurNAc-L-Ala-D-Glu (By similarity).
BINDING 390 390 Meso-diaminopimelate (By similarity).
BINDING 465 465 Meso-diaminopimelate; via carbonyl oxygen
BINDING 469 469 Meso-diaminopimelate (By similarity).
MOD_RES 225 225 N6-carboxylysine (By similarity). |
Keyword | ATP-binding; Cell cycle; Cell division; Cell shape; Cell wall biogenesis/degradation; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; Peptidoglycan synthesis; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 495 AA |
Protein Sequence | MADRNLRDLL APWVAGLPAR ELREMTLDSR VAAAGDLFVA VVGHQADGRR YIPQAIAQGV 60
AAIIAEAKDE ASDGEIREMH GVPVVYLSQL NERLSALAGR FYHEPSENMR LVAVTGTNGK 120
TTTTQLLAQW SQLLGETSAV MGTVGNGLLG KVIPTENTTG SAVDVQHVLA SLVAQGATFG 180
AMEVSSHGLV QHRVAALKFA ASVFTNLSRD HLDYHGDMAH YEAAKWMLYS THHHGQAIVN 240
ADDEVGRRWL ASLPDAVAVS MEGHINPNCH GRWLKAEAVE YHDRGATIRF ASSWGEGEIE 300
SRLMGAFNVS NLLLALATLL ALGYPLTDLL KTAARLQPVC GRMEVFTAPG KPTVVVDYAH 360
TPDALEKALQ AARLHCAGKL WCVFGCGGDR DKGKRPLMGA IAEEFADIVV VTDDNPRTEE 420
PRAIINDILA GMLDAGQVRV MEGRAEAVTN AIMQAKDNDV VLIAGKGHED YQIVGTQRLD 480
YSDRVTAARL LGVIA 495 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0005524; F:ATP binding; IEA:HAMAP. GO:0008765; F:UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase activity; IEA:HAMAP. GO:0007049; P:cell cycle; IEA:UniProtKB-KW. GO:0051301; P:cell division; IEA:UniProtKB-KW. GO:0009252; P:peptidoglycan biosynthetic process; IEA:HAMAP. GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |