ID A0A0Q8QXP3_9BURK Unreviewed; 464 AA.
AC A0A0Q8QXP3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=ASE07_17100 {ECO:0000313|EMBL:KRB90507.1};
OS Noviherbaspirillum sp. Root189.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Noviherbaspirillum.
OX NCBI_TaxID=1736487 {ECO:0000313|EMBL:KRB90507.1, ECO:0000313|Proteomes:UP000051303};
RN [1] {ECO:0000313|EMBL:KRB90507.1, ECO:0000313|Proteomes:UP000051303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root189 {ECO:0000313|EMBL:KRB90507.1,
RC ECO:0000313|Proteomes:UP000051303};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB90507.1, ECO:0000313|Proteomes:UP000051303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root189 {ECO:0000313|EMBL:KRB90507.1,
RC ECO:0000313|Proteomes:UP000051303};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KRB90507.1}.
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DR EMBL; LMHZ01000010; KRB90507.1; -; Genomic_DNA.
DR RefSeq; WP_057290142.1; NZ_LMHZ01000010.1.
DR AlphaFoldDB; A0A0Q8QXP3; -.
DR STRING; 1736487.ASE07_17100; -.
DR OrthoDB; 9804126at2; -.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000051303; 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:UP000051303}.
FT DOMAIN 2..100
FT /note="Mur ligase N-terminal catalytic"
FT /evidence="ECO:0000259|Pfam:PF01225"
FT DOMAIN 108..301
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 321..370
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
FT BINDING 110..116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02020"
SQ SEQUENCE 464 AA; 50185 MW; 17BC44F57A9DC318 CRC64;
MHIHILGICG TFMGGLAVLA KEAGHKVTGC DANVYPPMST QLQAQGIELI EGFAPDQVNL
QPDLFVIGNV VSRGNPLMEE ILNRGLAYVS GPQWIGEHIL RNKWVLSVAG THGKTTTSSM
LAWILEDAGY DPGFLIGGVP MNFGISARLS GKGKESSFFV IEADEYDTAF FDKRSKFVHY
RTKTAVLNNL EYDHADIFPD LGAIETQFHH LVRTVPGVGR LIVNGREESL RRVVARGCWS
DKEWFGTDAT NVIEGAAGWA LKTHEDDSFD VIFNGALQGT VNWSLTGEHN RMNALASIAA
ARHVGVTPAV AIEALQKFEN VKRRMEVRGT VTDITVYDDF AHHPTAIATT VAGLRKKVGN
ARILAVLEPR SNTMKLGTMK EALPGSLTDA DLVFGYGAKA GKDALGWNLS EALAPLGRNA
STYDELDTLV QAITRAARPG DHVLVMSNGG FGGVHQKILD ALAQ
//
