ID   MURE_CHLTA              Reviewed;         483 AA.
AC   Q3KM93;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   16-JUN-2009, entry version 30.
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=CTA_0291;
OS   Chlamydia trachomatis (strain A/HAR-13 / ATCC VR-571B).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydia.
OX   NCBI_TaxID=315277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16177312; DOI=10.1128/IAI.73.10.6407-6418.2005;
RA   Carlson J.H., Porcella S.F., McClarty G., Caldwell H.D.;
RT   "Comparative genomic analysis of Chlamydia trachomatis oculotropic and
RT   genitotropic strains.";
RL   Infect. Immun. 73:6407-6418(2005).
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; CP000051; AAX50529.1; -; Genomic_DNA.
DR   RefSeq; YP_328077.1; -.
DR   GeneID; 3687321; -.
DR   GenomeReviews; CP000051_GR; CTA_0291.
DR   KEGG; cta:CTA_0291; -.
DR   HOGENOM; Q3KM93; -.
DR   OMA; Q3KM93; FPVIVDY.
DR   BioCyc; CTRA315277-1:CTA_0291-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    483       UDP-N-acetylmuramoyl-L-alanyl-D-
FT                                glutamate--2,6-diaminopimelate ligase.
FT                                /FTId=PRO_1000012346.
FT   NP_BIND     109    115       ATP (Potential).
FT   REGION      151    152       UDP-MurNAc-L-Ala-D-Glu binding (By
FT                                similarity).
FT   REGION      403    406       Meso-diaminopimelate binding (By
FT                                similarity).
FT   MOTIF       403    406       Meso-diaminopimelate recognition motif.
FT   BINDING      30     30       UDP-MurNAc-L-Ala-D-Glu (By similarity).
FT   BINDING     178    178       UDP-MurNAc-L-Ala-D-Glu (By similarity).
FT   BINDING     186    186       UDP-MurNAc-L-Ala-D-Glu (By similarity).
FT   BINDING     380    380       Meso-diaminopimelate (By similarity).
FT   BINDING     453    453       Meso-diaminopimelate; via carbonyl oxygen
FT                                (By similarity).
FT   BINDING     457    457       Meso-diaminopimelate (By similarity).
FT   MOD_RES     218    218       N6-carboxylysine (By similarity).
SQ   SEQUENCE   483 AA;  53334 MW;  AFD354C9E5F3FC95 CRC64;
     MHLDQLLQNI PAKIYGKVES IPVRNLTRDS RCVGVGDIFI ARQGQFCNGN DYSSQAVANG
     AIAVLSSLYN PFLSVVQIIA EDPIALEASL AARFYNNPSR HLDVIGITGT NGKTTVSCLV
     RELMERSGRR TGLIGTIEHI LGENRIIDSF TTPDAILLQK YFAEMVKQNL SAAVMEVSSI
     GMALGRVRET EFLAGVLTNI TSDHLDFHGS LEEYIAAKKQ FFASLPEKGI AVVNLDCEYA
     PSFLNGSQAR AVSYAIHQEA DYRADRLKLY SSGSSYDIWY QGQVFPCETS LIGEHNVYNV
     LASLAVVHQF LGRDFADLVR DVRFLSAPKG RLDPILLGPF PVYIDYAHTP DALDNVCRIL
     LQLLPKDGRL IIVFGCGGDR DRVKRPLMAK VSEHYGFSFV TSDNPRTEDP DQIIADICKG
     FSTDHYVVES DRKLAIEKAI SMASDKDIVL VAGKGHEGYQ IFKHQTIVFD DREVVCEALA
     ALC
//