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Database: UniProt
Entry: Q8KGC9
LinkDB: Q8KGC9
Original site: Q8KGC9 
ID   MURE_CHLTE              Reviewed;         508 AA.
AC   Q8KGC9;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-APR-2014, entry version 88.
DE   RecName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase;
DE            EC=6.3.2.13;
DE   AltName: Full=Meso-A2pm-adding enzyme;
DE   AltName: Full=Meso-diaminopimelate-adding enzyme;
DE   AltName: Full=UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase;
DE   AltName: Full=UDP-MurNAc-tripeptide synthetase;
DE   AltName: Full=UDP-N-acetylmuramyl-tripeptide synthetase;
GN   Name=murE; OrderedLocusNames=CT0039;
OS   Chlorobium tepidum (strain ATCC 49652 / DSM 12025 / TLS).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobaculum.
OX   NCBI_TaxID=194439;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49652 / DSM 12025 / TLS;
RX   PubMed=12093901; DOI=10.1073/pnas.132181499;
RA   Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M.,
RA   Dodson R.J., DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Durkin A.S., Kolonay J.F., Yang F.,
RA   Holt I.E., Umayam L.A., Mason T.M., Brenner M., Shea T.P.,
RA   Parksey D.S., Nierman W.C., Feldblyum T.V., Hansen C.L., Craven M.B.,
RA   Radune D., Vamathevan J.J., Khouri H.M., White O., Gruber T.M.,
RA   Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A., Fraser C.M.;
RT   "The complete genome sequence of Chlorobium tepidum TLS, a
RT   photosynthetic, anaerobic, green-sulfur bacterium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
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; AE006470; AAM71287.1; -; Genomic_DNA.
DR   RefSeq; NP_660945.1; NC_002932.3.
DR   ProteinModelPortal; Q8KGC9; -.
DR   STRING; 194439.CT0039; -.
DR   EnsemblBacteria; AAM71287; AAM71287; CT0039.
DR   GeneID; 1006457; -.
DR   KEGG; cte:CT0039; -.
DR   PATRIC; 21398179; VBIChlTep116050_0038.
DR   eggNOG; COG0769; -.
DR   HOGENOM; HOG000268118; -.
DR   KO; K01928; -.
DR   OMA; KIKMIGN; -.
DR   OrthoDB; EOG6PKFCR; -.
DR   ProtClustDB; CLSK637122; -.
DR   BioCyc; CTEP194439:GHN0-40-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:InterPro.
DR   GO; GO:0008765; F:UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.1190.10; -; 1.
DR   Gene3D; 3.40.1390.10; -; 1.
DR   Gene3D; 3.90.190.20; -; 1.
DR   HAMAP; MF_00208; MurE; 1.
DR   InterPro; IPR018109; Folylpolyglutamate_synth_CS.
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   Pfam; PF01225; Mur_ligase; 1.
DR   Pfam; PF02875; Mur_ligase_C; 1.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   SUPFAM; SSF53244; SSF53244; 1.
DR   SUPFAM; SSF53623; SSF53623; 1.
DR   SUPFAM; SSF63418; SSF63418; 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;
KW   Reference proteome.
FT   CHAIN         1    508       UDP-N-acetylmuramoyl-L-alanyl-D-
FT                                glutamate--2,6-diaminopimelate ligase.
FT                                /FTId=PRO_0000101882.
FT   NP_BIND     124    130       ATP (Potential).
FT   REGION      166    167       UDP-MurNAc-L-Ala-D-Glu binding (By
FT                                similarity).
FT   REGION      428    431       Meso-diaminopimelate binding (By
FT                                similarity).
FT   MOTIF       428    431       Meso-diaminopimelate recognition motif.
FT   BINDING      43     43       UDP-MurNAc-L-Ala-D-Glu (By similarity).
FT   BINDING     193    193       UDP-MurNAc-L-Ala-D-Glu (By similarity).
FT   BINDING     201    201       UDP-MurNAc-L-Ala-D-Glu (By similarity).
FT   BINDING     404    404       Meso-diaminopimelate (By similarity).
FT   BINDING     478    478       Meso-diaminopimelate; via carbonyl oxygen
FT                                (By similarity).
FT   BINDING     482    482       Meso-diaminopimelate (By similarity).
FT   MOD_RES     233    233       N6-carboxylysine (By similarity).
SQ   SEQUENCE   508 AA;  54302 MW;  0744F64F4B4E9490 CRC64;
     MKEIREGAPG AQLDDLVAAL GALAERRGGD GARAVITGVT CDSRAVTPGA LFVAVRGLVA
     DGHHFIGAAI EAGAVAVACE ELPAAYSDSV TWLVVPDARK ALAELSKAFY GNASDKLMLI
     GVTGTNGKTT TARLVTSMLN ASGVAAGYIG TGLCRIGNHD IPLERTTPEP NRLHDLFRQM
     VDAGCRAAVM EVSSHSLVLD RVHGLFFRAA VFTNLTPEHL DFHETMEEYA EAKRLLFDQL
     NAEGFAVINA DDPRAEFMAA RLAPERVFCC STGDNTSLCD PARRFHAVIT ASTVEGSKAD
     VTFDGQSMAM QVPLPGAYNV MNMLEAFTVG VGLGIDPATA LRSLAAADAI AGRMERIWSR
     DRSRCAVVDY AHTPDALQKA LEALRAVTPA DAKLAVVFGC GGNRDRQKRP EMGRIAAELA
     DRVILTSDNP RDENPEAILD EVEAGMAGRV HLRIADRAEA IRRAVEQLGA GDILLVAGKG
     HEAYQEIRGV KHHFSDRECL EACFAQMK
//
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