ID   A0A2D6WN19_9BACT        Unreviewed;       499 AA.
AC   A0A2D6WN19;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   12-SEP-2018, entry version 4.
DE   RecName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase {ECO:0000256|HAMAP-Rule:MF_00208};
DE            EC=6.3.2.13 {ECO:0000256|HAMAP-Rule:MF_00208};
DE   AltName: Full=Meso-A2pm-adding enzyme {ECO:0000256|HAMAP-Rule:MF_00208};
DE   AltName: Full=Meso-diaminopimelate-adding enzyme {ECO:0000256|HAMAP-Rule:MF_00208};
DE   AltName: Full=UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase {ECO:0000256|HAMAP-Rule:MF_00208};
DE   AltName: Full=UDP-MurNAc-tripeptide synthetase {ECO:0000256|HAMAP-Rule:MF_00208};
DE   AltName: Full=UDP-N-acetylmuramyl-tripeptide synthetase {ECO:0000256|HAMAP-Rule:MF_00208};
GN   Name=murE {ECO:0000256|HAMAP-Rule:MF_00208};
GN   ORFNames=CML08_01500 {ECO:0000313|EMBL:MAH40063.1};
OS   Puniceicoccaceae bacterium.
OC   Bacteria; Verrucomicrobia; Opitutae; Puniceicoccales;
OC   Puniceicoccaceae.
OX   NCBI_TaxID=2026784 {ECO:0000313|EMBL:MAH40063.1};
RN   [1] {ECO:0000313|EMBL:MAH40063.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARS1008 {ECO:0000313|EMBL:MAH40063.1};
RA   Tully B.J., Graham E.D., Heidelberg J.F.;
RT   "The Reconstruction of 2,631 Draft Metagenome-Assembled Genomes from
RT   the Global Oceans.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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       {ECO:0000256|HAMAP-Rule:MF_00208}.
CC   -!- CATALYTIC ACTIVITY: ATP + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-
CC       D-glutamate + meso-2,6-diaminoheptanedioate = ADP + phosphate +
CC       UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6-
CC       diaminoheptanedioate. {ECO:0000256|HAMAP-Rule:MF_00208}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00208};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00208, ECO:0000256|RuleBase:RU004135,
CC       ECO:0000256|SAAS:SAAS00951514}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00208,
CC       ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951526}.
CC   -!- PTM: Carbamoylation is probably crucial for Mg(2+) binding and,
CC       consequently, for the gamma-phosphate positioning of ATP.
CC       {ECO:0000256|HAMAP-Rule:MF_00208}.
CC   -!- SIMILARITY: Belongs to the MurCDEF family. MurE subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00208, ECO:0000256|SAAS:SAAS00569976}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00208}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:MAH40063.1}.
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DR   EMBL; NZEM01000022; MAH40063.1; -; Genomic_DNA.
DR   UniPathway; UPA00219; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008765; F:UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.1190.10; -; 1.
DR   Gene3D; 3.90.190.20; -; 1.
DR   HAMAP; MF_00208; MurE; 1.
DR   InterPro; IPR036565; Mur-like_cat_sf.
DR   InterPro; IPR004101; Mur_ligase_C.
DR   InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   InterPro; IPR000713; Mur_ligase_N.
DR   InterPro; IPR035911; MurE/MurF_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 {ECO:0000256|HAMAP-Rule:MF_00208,
KW   ECO:0000256|SAAS:SAAS00951530};
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_00208,
KW   ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951553};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_00208,
KW   ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951537};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_00208,
KW   ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951545};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00208,
KW   ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951523};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00208,
KW   ECO:0000256|SAAS:SAAS00951519};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00208,
KW   ECO:0000256|SAAS:SAAS00951534, ECO:0000313|EMBL:MAH40063.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00208};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00208,
KW   ECO:0000256|SAAS:SAAS00951542};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00208,
KW   ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951548}.
FT   DOMAIN       26     96       Mur_ligase. {ECO:0000259|Pfam:PF01225}.
FT   DOMAIN      108    313       Mur_ligase_M. {ECO:0000259|Pfam:PF08245}.
FT   DOMAIN      333    414       Mur_ligase_C. {ECO:0000259|Pfam:PF02875}.
FT   NP_BIND     110    116       ATP. {ECO:0000256|HAMAP-Rule:MF_00208}.
FT   REGION      151    152       UDP-MurNAc-L-Ala-D-Glu binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00208}.
FT   REGION      408    411       Meso-diaminopimelate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00208}.
FT   MOTIF       408    411       Meso-diaminopimelate recognition motif.
FT                                {ECO:0000256|HAMAP-Rule:MF_00208}.
FT   BINDING      30     30       UDP-MurNAc-L-Ala-D-Glu.
FT                                {ECO:0000256|HAMAP-Rule:MF_00208}.
FT   BINDING     178    178       UDP-MurNAc-L-Ala-D-Glu.
FT                                {ECO:0000256|HAMAP-Rule:MF_00208}.
FT   BINDING     184    184       UDP-MurNAc-L-Ala-D-Glu.
FT                                {ECO:0000256|HAMAP-Rule:MF_00208}.
FT   BINDING     186    186       UDP-MurNAc-L-Ala-D-Glu.
FT                                {ECO:0000256|HAMAP-Rule:MF_00208}.
FT   BINDING     384    384       Meso-diaminopimelate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00208}.
FT   BINDING     462    462       Meso-diaminopimelate; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00208}.
FT   BINDING     466    466       Meso-diaminopimelate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00208}.
FT   MOD_RES     218    218       N6-carboxylysine. {ECO:0000256|HAMAP-
FT                                Rule:MF_00208}.
SQ   SEQUENCE   499 AA;  54410 MW;  5CBC2B63ADD92B3D CRC64;
     MKLKEVLSEI EVLDYRLGAA AECTALLTDS RRAVSGGLFF AISGRKNDGN DYIEQAVDRG
     VVAVVTEQAL GKHFPIDYIQ VPDVRIALAK IAKLFYGSPD RSLAITGITG TNGKTTVSML
     AQHLLGGSQS VGLIGTIRYD IGKRTLPSHR TTPESPDCFQ LFSEMREVGS KAAVMEVSSH
     GIDQCRVHYI EMDTVVFLNL SRDHMDYHPT IEDYFQVKQR LFTGALGTAA KRAIVNADCP
     YGQKILADLG LESATKALSF GLNAGADFRA IDLCLASGDT RFTFVYPEGQ IEVYSPLIGR
     HNVYNTLAAL AIAYVQGCSL VDCVEALVSF PGVPGRMEQI QAGQDFSVLV DYAHTADAIE
     HTCEMLRELS RGKKIIVFGC GGDRDRGKRP LMMRAALNGA DTVIVTADNP RTEAIESIFQ
     DMRSGIESEA EAERVQFIVD RKNACARAFE SASAGDCVLI AGKGHEVYQE IQGTMMPFDD
     RKVARELLEN RGASKLDLN
//