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 01-MAY-2013, entry version 83.
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; HTMEEYA; -.
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: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: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:HAMAP.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0046901; P:tetrahydrofolylpolyglutamate biosynthetic process; IEA:GOC.
DR Gene3D; 3.40.1190.10; -; 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; Mur_ligase_C; 1.
DR SUPFAM; SSF53623; Mur_ligase_cen; 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
//
