ID   MURE_CYTH3              Reviewed;         486 AA.
AC   Q11RG9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   16-JUN-2009, entry version 27.
DE   RecName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase;
DE            EC=6.3.2.13;
DE   AltName: Full=UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase;
DE   AltName: Full=Meso-diaminopimelate-adding enzyme;
DE   AltName: Full=Meso-A2pm-adding enzyme;
DE   AltName: Full=UDP-N-acetylmuramyl-tripeptide synthetase;
DE   AltName: Full=UDP-MurNAc-tripeptide synthetase;
GN   Name=murE; OrderedLocusNames=CHU_2745;
OS   Cytophaga hutchinsonii (strain ATCC 33406 / NCIMB 9469).
OC   Bacteria; Bacteroidetes; Sphingobacteria; Sphingobacteriales;
OC   Flexibacteraceae; Cytophaga.
OX   NCBI_TaxID=269798;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17400776; DOI=10.1128/AEM.00225-07;
RA   Xie G., Bruce D.C., Challacombe J.F., Chertkov O., Detter J.C.,
RA   Gilna P., Han C.S., Lucas S., Misra M., Myers G.L., Richardson P.,
RA   Tapia R., Thayer N., Thompson L.S., Brettin T.S., Henrissat B.,
RA   Wilson D.B., McBride M.J.;
RT   "Genome sequence of the cellulolytic gliding bacterium Cytophaga
RT   hutchinsonii.";
RL   Appl. Environ. Microbiol. 73:3536-3546(2007).
CC   -!- FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to
CC       the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate
CC       (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + UDP-N-acetylmuramoyl-L-alanyl-D-
CC       glutamate + meso-2,6-diaminoheptanedioate = ADP + phosphate + UDP-
CC       N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6-diamino-
CC       heptanedioate.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- PTM: Carbamoylation is probably crucial for Mg(2+) binding and,
CC       consequently, for the gamma-phosphate positioning of ATP (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the murCDEF family. MurE subfamily.
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DR   EMBL; CP000383; ABG59995.1; -; Genomic_DNA.
DR   RefSeq; YP_679337.1; -.
DR   GeneID; 4185335; -.
DR   GenomeReviews; CP000383_GR; CHU_2745.
DR   KEGG; chu:CHU_2745; -.
DR   NMPDR; fig|269798.12.peg.2634; -.
DR   HOGENOM; Q11RG9; -.
DR   OMA; Q11RG9; HTPDGIE.
DR   BioCyc; CHUT269798:CHU_2745-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0008765; F:UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-...; IEA:EC.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007047; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:HAMAP.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   HAMAP; MF_00208; -; 1.
DR   InterPro; IPR004101; Mur_ligase_C.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   InterPro; IPR000713; Mur_ligase_N.
DR   InterPro; IPR005761; UDP-N-AcMur-Glu-dNH2Pim_ligase.
DR   Gene3D; G3DSA:3.90.190.20; Mur_ligase_C; 1.
DR   Gene3D; G3DSA:3.40.1190.10; Mur_ligase_cen; 1.
DR   Pfam; PF01225; Mur_ligase; 1.
DR   Pfam; PF02875; Mur_ligase_C; 1.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   TIGRFAMs; TIGR01085; murE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell cycle; Cell division; Cell shape;
KW   Cell wall biogenesis/degradation; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Peptidoglycan synthesis.
FT   CHAIN         1    486       UDP-N-acetylmuramoyl-L-alanyl-D-
FT                                glutamate--2,6-diaminopimelate ligase.
FT                                /FTId=PRO_1000012350.
FT   NP_BIND     112    118       ATP (Potential).
FT   REGION      154    155       UDP-MurNAc-L-Ala-D-Glu binding (By
FT                                similarity).
FT   REGION      402    405       Meso-diaminopimelate binding (By
FT                                similarity).
FT   MOTIF       402    405       Meso-diaminopimelate recognition motif.
FT   BINDING      30     30       UDP-MurNAc-L-Ala-D-Glu (By similarity).
FT   BINDING     181    181       UDP-MurNAc-L-Ala-D-Glu (By similarity).
FT   BINDING     187    187       UDP-MurNAc-L-Ala-D-Glu (By similarity).
FT   BINDING     189    189       UDP-MurNAc-L-Ala-D-Glu (By similarity).
FT   BINDING     378    378       Meso-diaminopimelate (By similarity).
FT   BINDING     455    455       Meso-diaminopimelate; via carbonyl oxygen
FT                                (By similarity).
FT   BINDING     459    459       Meso-diaminopimelate (By similarity).
FT   MOD_RES     221    221       N6-carboxylysine (By similarity).
SQ   SEQUENCE   486 AA;  53279 MW;  2FB7EB012E12EAF1 CRC64;
     MQIKDLIYKV SLISVSGRTD VDVTAICFDS RKVEKGSMFI AVRGVSSDGH SFIADVIQKG
     ATAVVCEELP EIESTADCTI IQVKDSAEAL GMIASNFYDS PSSKLKLVGV TGTNGKTTTV
     TLLYRLFRKL GYKTGLLSTV ENIIEDKVVQ ATHTTPDAIS LNKLLADMVK AGCTHCFMEV
     SSHAAVQRRI AGLQFAGGLF SNITHDHLDY HKTFDEYIKA KKLFFDGLPN DSFALINSDD
     KRGRVMIQNT RAKTYTYSLL ALADFKGKLI STTMQGLEMD VDGIQAWFRL IGNFNAYNLL
     AVYATAVLLG EDKEEVLMQL STIEAANGRF EQQISATRIT VIVDYAHTPD ALKNVLETIT
     ELKGANKIIT VVGCGGNRDA AKRPVMADIA CQFSDHVVLT SDNPRNEEPQ AILTEMEKGV
     RIVDKKKVLS VLDRKEAIKV ACTLASTGDI ILVAGKGHET YQEIKGVKYP FDDRLIIKEL
     LDTLGK
//