ID   A0A9D5RKK9_9FIRM        Unreviewed;       769 AA.
AC   A0A9D5RKK9;
DT   03-MAY-2023, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2023, sequence version 1.
DT   24-JUL-2024, entry version 7.
DE   RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00197, ECO:0000256|HAMAP-Rule:MF_00208};
DE   Includes:
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};
DE   Includes:
DE     RecName: Full=Diaminopimelate epimerase {ECO:0000256|HAMAP-Rule:MF_00197};
DE              Short=DAP epimerase {ECO:0000256|HAMAP-Rule:MF_00197};
DE              EC=5.1.1.7 {ECO:0000256|HAMAP-Rule:MF_00197};
DE     AltName: Full=PLP-independent amino acid racemase {ECO:0000256|HAMAP-Rule:MF_00197};
GN   Name=murE {ECO:0000256|HAMAP-Rule:MF_00208};
GN   Synonyms=dapF {ECO:0000256|HAMAP-Rule:MF_00197};
GN   ORFNames=E7269_00350 {ECO:0000313|EMBL:MBE5921199.1};
OS   Lachnospiraceae bacterium.
OC   Bacteria; Bacillota; Clostridia; Lachnospirales; Lachnospiraceae.
OX   NCBI_TaxID=1898203 {ECO:0000313|EMBL:MBE5921199.1, ECO:0000313|Proteomes:UP000806229};
RN   [1] {ECO:0000313|EMBL:MBE5921199.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SIG308 {ECO:0000313|EMBL:MBE5921199.1};
RA   Peng X.;
RT   "Evolution of Biomass-Degrading Anaerobic Consortia Revealed by
RT   Metagenomics.";
RL   Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the
CC       nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG)
CC       in the biosynthesis of bacterial cell-wall peptidoglycan.
CC       {ECO:0000256|HAMAP-Rule:MF_00208}.
CC   -!- FUNCTION: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate
CC       (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-
CC       lysine and an essential component of the bacterial peptidoglycan.
CC       {ECO:0000256|HAMAP-Rule:MF_00197}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2S,6S)-2,6-diaminoheptanedioate = meso-2,6-
CC         diaminoheptanedioate; Xref=Rhea:RHEA:15393, ChEBI:CHEBI:57609,
CC         ChEBI:CHEBI:57791; EC=5.1.1.7; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00197};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + meso-2,6-diaminoheptanedioate + 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-2,6-
CC         diaminoheptanedioate; 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;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00208};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_00197}.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752, ECO:0000256|HAMAP-Rule:MF_00208,
CC       ECO:0000256|RuleBase:RU004135}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00197}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00197,
CC       ECO:0000256|RuleBase:RU004135}.
CC   -!- PTM: Carboxylation 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|ARBA:ARBA00005898, ECO:0000256|HAMAP-Rule:MF_00208}.
CC   -!- SIMILARITY: Belongs to the diaminopimelate epimerase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00197}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00197}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:MBE5921199.1}.
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DR   EMBL; SVEO01000001; MBE5921199.1; -; Genomic_DNA.
DR   Proteomes; UP000806229; 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:0008837; F:diaminopimelate epimerase activity; 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:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniRule.
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; 3.90.190.20; Mur ligase, C-terminal domain; 1.
DR   Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR   Gene3D; 3.40.1390.10; MurE/MurF, N-terminal domain; 1.
DR   HAMAP; MF_00197; DAP_epimerase; 1.
DR   HAMAP; MF_00208; MurE; 1.
DR   InterPro; IPR018510; DAP_epimerase_AS.
DR   InterPro; IPR001653; DAP_epimerase_DapF.
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   NCBIfam; TIGR00652; DapF; 1.
DR   NCBIfam; TIGR01085; murE; 1.
DR   PANTHER; PTHR23135; MUR LIGASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR23135:SF4; UDP-N-ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE--2,6-DIAMINOPIMELATE LIGASE MURE HOMOLOG, CHLOROPLASTIC; 1.
DR   Pfam; PF01678; DAP_epimerase; 2.
DR   Pfam; PF01225; Mur_ligase; 1.
DR   Pfam; PF02875; Mur_ligase_C; 1.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   SUPFAM; SSF54506; Diaminopimelate epimerase-like; 2.
DR   SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR   SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
DR   SUPFAM; SSF63418; MurE/MurF N-terminal domain; 1.
DR   PROSITE; PS01326; DAP_EPIMERASE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00197};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00208};
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW   Rule:MF_00208};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW   Rule:MF_00208};
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW   Rule:MF_00208};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW   ECO:0000256|HAMAP-Rule:MF_00208};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00197};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_00197};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00208};
KW   Lysine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00197};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00208};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00208};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP-
KW   Rule:MF_00208}.
FT   DOMAIN          23..95
FT                   /note="Mur ligase N-terminal catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01225"
FT   DOMAIN          108..309
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          329..410
FT                   /note="Mur ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02875"
FT   MOTIF           404..407
FT                   /note="Meso-diaminopimelate recognition motif"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
FT   ACT_SITE        560
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10125"
FT   ACT_SITE        560
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   ACT_SITE        712
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   BINDING         30
FT                   /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT                   glutamate"
FT                   /ligand_id="ChEBI:CHEBI:83900"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
FT   BINDING         110..116
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
FT   BINDING         151
FT                   /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT                   glutamate"
FT                   /ligand_id="ChEBI:CHEBI:83900"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
FT   BINDING         152..153
FT                   /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT                   glutamate"
FT                   /ligand_id="ChEBI:CHEBI:83900"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
FT   BINDING         179
FT                   /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT                   glutamate"
FT                   /ligand_id="ChEBI:CHEBI:83900"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
FT   BINDING         187
FT                   /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT                   glutamate"
FT                   /ligand_id="ChEBI:CHEBI:83900"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
FT   BINDING         380
FT                   /ligand="meso-2,6-diaminoheptanedioate"
FT                   /ligand_id="ChEBI:CHEBI:57791"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
FT   BINDING         404..407
FT                   /ligand="meso-2,6-diaminoheptanedioate"
FT                   /ligand_id="ChEBI:CHEBI:57791"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
FT   BINDING         456
FT                   /ligand="meso-2,6-diaminoheptanedioate"
FT                   /ligand_id="ChEBI:CHEBI:57791"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
FT   BINDING         460
FT                   /ligand="meso-2,6-diaminoheptanedioate"
FT                   /ligand_id="ChEBI:CHEBI:57791"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
FT   BINDING         496
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   BINDING         551
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   BINDING         561..562
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   BINDING         652
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   BINDING         685
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   BINDING         703..704
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   BINDING         713..714
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   SITE            654
FT                   /note="Could be important to modulate the pK values of the
FT                   two catalytic cysteine residues"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   SITE            703
FT                   /note="Could be important to modulate the pK values of the
FT                   two catalytic cysteine residues"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   MOD_RES         221
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
SQ   SEQUENCE   769 AA;  84898 MW;  EFCA6B02CCDA00B2 CRC64;
     MLLKELLSEI TYEVLQGTTD TDVTELVYDS RKASVGCVFL CISGTTVDAH DFIPQVAEKG
     AAAIVVTKDV QVPANVTVVK VENARKALSY MAAAYFGKPA EKMTLIGITG TKGKTTTSYM
     VQAMLEMAGK KVGVIGTIGA VIDKGIVKTS NTTPESYEVQ RLFAKMVEAG CEYCIMEVSS
     QGMKMDRVAG VLFDYGIFTN FSSDHIGPNE HADMAEYLYC KSLLFRQCKV GIINRDSEYW
     QGVTEGHTCE LKTYGFDADA DLRGANQKLV RKSGVLGVEF DVEGVLNCHV KTCIPGRFSV
     YNCLTALAIG WHLDIPIEAM THALKNIRVP GRVELVDISP KFTIMVDYAH NAMSVESLLT
     TIKEYNPNRI ICVYGLGGNR SKVRRYEVGE LCGKMADLSV LTADNPRNEE IADIFNDIKI
     GLAKTNGKYI EIPDRKEAIY YAIDHAQEND IIVVFGKGHE DYQEIKGVRY PYNDKEAILS
     YLKREMNFVK LHGCGNPYIY MDVRGKNYEN AFLQALSIKV SDKSKGIGAD GLIVLDDAQT
     EGTDGRMRMF NADGSEGAMC GNGIRCLAKF MYEHAGIEKE HMVIETKSGL REVDLIHEGD
     EITKATVYMG HPEFEAANVP VISEHPVFMD GELPVELESG VKYCGTCMSM GNPHCVIFTE
     DIDALELAKI GPKFECHEMF PERVNTEFIE IVDRNNVRMR VWERGSGETM ACGTGACAVV
     AAGVRTGRLS NKVNVMMRGG TLEITYDVEN NDIYMTGEAV QICVGKLRV
//