ID   A0A2K2FPK1_9FIRM        Unreviewed;       487 AA.
AC   A0A2K2FPK1;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   16-JAN-2019, entry version 9.
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=CDQ84_04540 {ECO:0000313|EMBL:PNU00706.1};
OS   Pseudoclostridium thermosuccinogenes.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales;
OC   Hungateiclostridiaceae; Pseudoclostridium.
OX   NCBI_TaxID=84032 {ECO:0000313|EMBL:PNU00706.1, ECO:0000313|Proteomes:UP000236151};
RN   [1] {ECO:0000313|EMBL:PNU00706.1, ECO:0000313|Proteomes:UP000236151}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5806 {ECO:0000313|EMBL:PNU00706.1,
RC   ECO:0000313|Proteomes:UP000236151};
RA   Koendjbiharie J.G., van Kranenburg R.;
RT   "Investigating the central metabolism of Clostridium
RT   thermosuccinogenes.";
RL   Submitted (JUN-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:
CC       Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-
CC         muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-
CC         acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-
CC         diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791,
CC         ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216;
CC         EC=6.3.2.13; Evidence={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:SAAS00354031}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00208,
CC       ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00354145}.
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:PNU00706.1}.
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DR   EMBL; NIOJ01000007; PNU00706.1; -; Genomic_DNA.
DR   KEGG; cthd:CDO33_06550; -.
DR   KO; K01928; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000236151; Unassembled WGS sequence.
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:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:InterPro.
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; IPR018109; Folylpolyglutamate_synth_CS.
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.
DR   PROSITE; PS01011; FOLYLPOLYGLU_SYNT_1; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00208};
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_00208,
KW   ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00031715};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_00208,
KW   ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00431810};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_00208,
KW   ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00031753};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00208,
KW   ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00031725};
KW   Complete proteome {ECO:0000313|Proteomes:UP000236151};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00208,
KW   ECO:0000256|SAAS:SAAS00031717};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00208, ECO:0000313|EMBL:PNU00706.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00208};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00208};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00208,
KW   ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00031730};
KW   Reference proteome {ECO:0000313|Proteomes:UP000236151}.
FT   DOMAIN       23     72       Mur_ligase. {ECO:0000259|Pfam:PF01225}.
FT   DOMAIN      108    307       Mur_ligase_M. {ECO:0000259|Pfam:PF08245}.
FT   DOMAIN      326    412       Mur_ligase_C. {ECO:0000259|Pfam:PF02875}.
FT   NP_BIND     110    116       ATP. {ECO:0000256|HAMAP-Rule:MF_00208}.
FT   REGION      152    153       UDP-MurNAc-L-Ala-D-Glu binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00208}.
FT   REGION      401    404       Meso-diaminopimelate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00208}.
FT   MOTIF       401    404       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     179    179       UDP-MurNAc-L-Ala-D-Glu.
FT                                {ECO:0000256|HAMAP-Rule:MF_00208}.
FT   BINDING     187    187       UDP-MurNAc-L-Ala-D-Glu.
FT                                {ECO:0000256|HAMAP-Rule:MF_00208}.
FT   BINDING     377    377       Meso-diaminopimelate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00208}.
FT   BINDING     453    453       Meso-diaminopimelate; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00208}.
FT   BINDING     457    457       Meso-diaminopimelate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00208}.
FT   MOD_RES     221    221       N6-carboxylysine. {ECO:0000256|HAMAP-
FT                                Rule:MF_00208}.
SQ   SEQUENCE   487 AA;  53460 MW;  D0D3189788871C8E CRC64;
     MFLRDLVKGL KVLDVKGNLD IDISDIAYDS RKVKKGSLFV CIDGMTTDGH KYIPSALENG
     AAALLVQKDV TVEDGVTVVK IEDTRFGLAF VSDAFFGHPS QKLHLIGVTG TKGKTTTTYM
     IKSILEHSGQ KVGLVGTIAN MIGDEVLYAQ RTTPESYDLQ SLFEEMLEKG VTSATMEVSS
     QGLALDRVGC CDFDIGIFTN ITSDHIGPRE HKDFDDYLEA KAKLFRMCKK GVINIDDPHA
     QRIMEKAECE ITTFGIEKDA DIKAYDVVKH STGVDFKITS PWGNEPISVS IPGKFNVYNA
     LAAIGACALS GISMESIKAG LANVKVKGRA EVVETGRDFT VMIDYAHNAI SLENILTTIK
     DYAPGRVVCL FGCGGDRDKA RRFEMGEVSG RLADFTIITS DNPRTEDPDA IINDIETGIK
     RTTGKYIKIT ERREAIKYAI DNAQPKDIIL LAGKGHETYQ EFKDKTIHFD EREVVAEILE
     KKQAAGC
//