ID   MURE_HAES1              Reviewed;         495 AA.
AC   Q0I1D8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 28.
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=HS_0353;
OS   Haemophilus somnus (strain 129Pt) (Histophilus somni (strain 129Pt)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Histophilus.
OX   NCBI_TaxID=205914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17172329; DOI=10.1128/JB.01422-06;
RA   Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O.,
RA   Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N.,
RA   Xie G., Inzana T.J.;
RT   "Complete genome sequence of Haemophilus somnus (Histophilus somni)
RT   strain 129Pt and comparison to Haemophilus ducreyi 35000HP and
RT   Haemophilus influenzae Rd.";
RL   J. Bacteriol. 189:1890-1898(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; CP000436; ABI24631.1; -; Genomic_DNA.
DR   RefSeq; YP_718563.1; -.
DR   GeneID; 4239829; -.
DR   GenomeReviews; CP000436_GR; HS_0353.
DR   KEGG; hso:HS_0353; -.
DR   NMPDR; fig|205914.1.peg.124; -.
DR   HOGENOM; Q0I1D8; -.
DR   OMA; Q0I1D8; HTPDGIE.
DR   BioCyc; HSOM205914:HS_0353-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    495       UDP-N-acetylmuramoyl-L-alanyl-D-
FT                                glutamate--2,6-diaminopimelate ligase.
FT                                /FTId=PRO_1000012359.
FT   NP_BIND     117    123       ATP (Potential).
FT   REGION       45     47       UDP-MurNAc-L-Ala-D-Glu binding (By
FT                                similarity).
FT   REGION      159    160       UDP-MurNAc-L-Ala-D-Glu binding (By
FT                                similarity).
FT   REGION      418    421       Meso-diaminopimelate binding (By
FT                                similarity).
FT   MOTIF       418    421       Meso-diaminopimelate recognition motif.
FT   BINDING      28     28       UDP-MurNAc-L-Ala-D-Glu; via carbonyl
FT                                oxygen (By similarity).
FT   BINDING      30     30       UDP-MurNAc-L-Ala-D-Glu (By similarity).
FT   BINDING     158    158       UDP-MurNAc-L-Ala-D-Glu (By similarity).
FT   BINDING     186    186       UDP-MurNAc-L-Ala-D-Glu (By similarity).
FT   BINDING     192    192       UDP-MurNAc-L-Ala-D-Glu (By similarity).
FT   BINDING     194    194       UDP-MurNAc-L-Ala-D-Glu (By similarity).
FT   BINDING     394    394       Meso-diaminopimelate (By similarity).
FT   BINDING     469    469       Meso-diaminopimelate; via carbonyl oxygen
FT                                (By similarity).
FT   BINDING     473    473       Meso-diaminopimelate (By similarity).
FT   MOD_RES     226    226       N6-carboxylysine (By similarity).
SQ   SEQUENCE   495 AA;  54656 MW;  93B412FEA2CFAAA5 CRC64;
     MKKLTALWDI DEQLDSVHRD IELQEMILDS RLANTGCLFV AIKGHRVDGR EFIMQAIQNG
     ASAVLFETDL VEQHLTVSFE QNIPLIAYYE LSKHLSHIAD RFYSSPSQRL TLVGVTGTNG
     KTTIAQLLAQ WTQILGHTSA VMGTIGNGLF GQIKEASNTT GSAIEIQSSL DKFIRQGADF
     AAIEVSSHGL VQHRVEALTF RAGIFTNLSR DHLDYHHTME NYAQAKKRLF SELNCQHKIL
     NVDDEIGATW LIELSKDDPD VVAVSCRADY QPDTKNWLKA TALSFHSKGT TIEFASSWGN
     GILSSPLIGG FNVSNLLLVL ATLLSLGYDI GKLLATVRQL TGVCGRMEML SAKHKATVIV
     DYAHTPDALE NALQSAAVHC QGKLWCIFGC GGDRDRGKRP LMAAIAEKFA DSVIVTDDNP
     RTENPEQIMQ DILTGFQQSS AVQIIHQREQ AIKTALQSAV ENDVVLIAGK GHENYQIIGT
     TKYHFSDQEI VKKYF
//