ID A0A165T993_9GAMM Unreviewed; 441 AA.
AC A0A165T993;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=UDP-N-acetylmuramate--L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptandioate ligase {ECO:0000256|HAMAP-Rule:MF_02020};
DE EC=6.3.2.45 {ECO:0000256|HAMAP-Rule:MF_02020};
DE AltName: Full=Murein peptide ligase {ECO:0000256|HAMAP-Rule:MF_02020};
DE AltName: Full=UDP-N-acetylmuramate:L-alanyl-gamma-D-glutamyl-meso-diaminopimelate ligase {ECO:0000256|HAMAP-Rule:MF_02020};
GN Name=mpl {ECO:0000256|HAMAP-Rule:MF_02020};
GN ORFNames=A3709_04105 {ECO:0000313|EMBL:KZX57176.1};
OS Halioglobus sp. HI00S01.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC Halioglobus.
OX NCBI_TaxID=1822214 {ECO:0000313|EMBL:KZX57176.1, ECO:0000313|Proteomes:UP000077184};
RN [1] {ECO:0000313|EMBL:KZX57176.1, ECO:0000313|Proteomes:UP000077184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HI00S01 {ECO:0000313|EMBL:KZX57176.1,
RC ECO:0000313|Proteomes:UP000077184};
RA Sosa O.A.;
RT "Microbial cycling of marine high molecular weight dissolved organic
RT matter.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Reutilizes the intact tripeptide L-alanyl-gamma-D-glutamyl-
CC meso-diaminopimelate by linking it to UDP-N-acetylmuramate.
CC {ECO:0000256|HAMAP-Rule:MF_02020}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-alanyl-gamma-D-glutamyl-meso-diaminoheptanedioate +
CC UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-
CC acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-
CC diaminoheptanedioate; Xref=Rhea:RHEA:29563, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:61401,
CC ChEBI:CHEBI:70757, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216;
CC EC=6.3.2.45; Evidence={ECO:0000256|HAMAP-Rule:MF_02020};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02020};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
CC {ECO:0000256|HAMAP-Rule:MF_02020}.
CC -!- SIMILARITY: Belongs to the MurCDEF family. Mpl subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_02020}.
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:KZX57176.1}.
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DR EMBL; LWEE01000110; KZX57176.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165T993; -.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000077184; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0106418; F:UDP-N-acetylmuramate-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate ligase activity; IEA:UniProtKB-EC.
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-KW.
DR GO; GO:0009254; P:peptidoglycan turnover; 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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR HAMAP; MF_02020; Mpl; 1.
DR InterPro; IPR005757; Mpl.
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 NCBIfam; TIGR01081; mpl; 1.
DR PANTHER; PTHR43445; UDP-N-ACETYLMURAMATE--L-ALANINE LIGASE-RELATED; 1.
DR PANTHER; PTHR43445:SF5; UDP-N-ACETYLMURAMATE--L-ALANYL-GAMMA-D-GLUTAMYL-MESO-2,6-DIAMINOHEPTANDIOATE LIGASE; 1.
DR Pfam; PF01225; Mur_ligase; 1.
DR Pfam; PF02875; Mur_ligase_C; 1.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR SUPFAM; SSF51984; MurCD N-terminal domain; 1.
DR SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_02020};
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW Rule:MF_02020};
KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW Rule:MF_02020};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW Rule:MF_02020};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW ECO:0000256|HAMAP-Rule:MF_02020};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02020};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_02020};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_02020};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP-
KW Rule:MF_02020}; Reference proteome {ECO:0000313|Proteomes:UP000077184}.
FT DOMAIN 1..87
FT /note="Mur ligase N-terminal catalytic"
FT /evidence="ECO:0000259|Pfam:PF01225"
FT DOMAIN 97..281
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 301..365
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
FT BINDING 98..104
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02020"
SQ SEQUENCE 441 AA; 47342 MW; 142AA123C2CF8AEC CRC64;
MGGIALLARE LGFEVTGSDA NVYPPMSTQL EAAGITLMEG YHPEHLQPAP DCVVVGNAMT
RGNPAVEYML DQGLAYTSGP QWLAENLLQG RWVLAASGTH GKTSTSSMLA WILEYAGMAP
GFLIGGVPAD FGLSARLGDT DFFVVEADEY DTAFFDKRSK FVHYRPRTLI INNLEFDHAD
IFPNLAAIQR QFHHVVRCVP ALGRIVHPAH SGAVATTLNM GCWTPRVSFA AGDDGDWSAQ
LLAADGSAFR VSSPRAEDVE VRWSHCGNHN VENALAAMAA AEHVGVVPPV AAQALGEFRG
IKRRLEHLGT AAGVAVYDDF AHHPTAIATT LAGMRARHNG GRLLALIEPR SNTMRMGEHR
ERLAPSTADA DRVYWYQGAN VNWDMQDVVD ACGHASLSRD IDELVQQVTA QSEPGDSVVV
MSNGGFGGIH GKLLAALEAK A
//
