ID D0SZQ7_ACILW Unreviewed; 454 AA.
AC D0SZQ7;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 65.
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 ECO:0000313|EMBL:EEY88542.1};
GN ORFNames=HMPREF0017_02781 {ECO:0000313|EMBL:EEY88542.1};
OS Acinetobacter lwoffii SH145.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=575588 {ECO:0000313|EMBL:EEY88542.1, ECO:0000313|Proteomes:UP000018425};
RN [1] {ECO:0000313|Proteomes:UP000018425}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH145 {ECO:0000313|Proteomes:UP000018425};
RX PubMed=23144699; DOI=10.1371/journal.pone.0046984;
RA Peleg A.Y., de Breij A., Adams M.D., Cerqueira G.M., Mocali S.,
RA Galardini M., Nibbering P.H., Earl A.M., Ward D.V., Paterson D.L.,
RA Seifert H., Dijkshoorn L.;
RT "The success of Acinetobacter species; genetic, metabolic and virulence
RT attributes.";
RL PLoS ONE 7:E46984-E46984(2012).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GG705069; EEY88542.1; -; Genomic_DNA.
DR RefSeq; WP_004281908.1; NZ_GG705069.1.
DR AlphaFoldDB; D0SZQ7; -.
DR eggNOG; COG0773; Bacteria.
DR HOGENOM; CLU_028104_0_1_6; -.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000018425; 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}.
FT DOMAIN 2..99
FT /note="Mur ligase N-terminal catalytic"
FT /evidence="ECO:0000259|Pfam:PF01225"
FT DOMAIN 108..295
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 315..363
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 454 AA; 49347 MW; 33EB600FCAD17585 CRC64;
MHLHILGICG TFMGSLALLA RDLGHQVTGS DLNVYPPMST QLENAGITLM QGYDRSHLQP
HPDLVIVGNA MKRGIDAVEY MLNAGLPYIS GPQFLADHVL QGKHVLGVAG THGKTTTTTM
LAWVLDQAGL EPGFLIGGVP LGFSESARLG GGKYFCVEAD EYDSAFFDKR SKFVHYHPKT
AILNNLEFDH ADIFDDLAAI QKQFHHLVRT IPSEGRIIAP ITESNIDEVL EQGCWTPVVR
TSLDANEKAK LYAEQLSADG SHFKVLQQGV VKGEVQWNMT GQHSVANALA TIAAAEHVGV
SIETACEALS NFGGVKRRME LLGTVRGIEV YDDFAHHPTA IDTTLEGARK RLGERKLWAI
IEPRSNTMRM GSHKDGLAHS ARLADEVIWY QPEGLDWDLQ PVIEAAPNKA KVARTLDDII
QTVVAEAGEG DAVVIMSNGG FGGLHQKLIT VLQA
//
