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Database: UniProt
Entry: A0A069I9Y7_9BURK
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ID   A0A069I9Y7_9BURK        Unreviewed;       462 AA.
AC   A0A069I9Y7;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 39.
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=CF70_025385 {ECO:0000313|EMBL:KDP83366.1};
OS   Cupriavidus sp. SK-3.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=1470558 {ECO:0000313|EMBL:KDP83366.1, ECO:0000313|Proteomes:UP000023560};
RN   [1] {ECO:0000313|EMBL:KDP83366.1, ECO:0000313|Proteomes:UP000023560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK-3 {ECO:0000313|EMBL:KDP83366.1,
RC   ECO:0000313|Proteomes:UP000023560};
RA   Vilo C., Benedik M.J., Ilori M., Dong Q.;
RT   "Cupriavidus sp. strain SK-3.";
RL   Submitted (MAY-2014) 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:KDP83366.1}.
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DR   EMBL; JFJV02000291; KDP83366.1; -; Genomic_DNA.
DR   RefSeq; WP_035875468.1; NZ_JFJV02000291.1.
DR   AlphaFoldDB; A0A069I9Y7; -.
DR   OrthoDB; 9804126at2; -.
DR   UniPathway; UPA00544; -.
DR   Proteomes; UP000023560; 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..100
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..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   462 AA;  49551 MW;  FC7EB7018ACF301E CRC64;
     MHIHILGICG TFMGGLAVLA KQAGHRVTGC DANVYPPMST QLEAQGIELI EGFDPNQLAL
     APDLFVIGNV VSRGNPLMEA ILNRNLPYTS GPQWLGEHVL RGKWTLAVAG THGKTTTTSM
     LAWILEDAGY NPGFLVGGVP QNFGVSARVT ESDFFVIEAD EYDTAFFDKR SKFVHYRPRT
     AILNNLEYDH ADIFPDLAAI ETQFHHLVRT VPEQGRLIVN GAEESLARVL ERGCWSETEQ
     FGMGDWRAGE PAGATGGAAQ DSFDVWFGEA LQGRLTWDLQ GTHNRLNALA AIAAARHVGV
     PPAQAIDSLS RFANVKRRME VRGVVDGITV YDDFAHHPTA IQTTLDGLRK RVGGARILAV
     LEPRSNTMKL GVMKAQLPAS LEAADLVFGY GAASGKDALG WDLAESLAPL GERAAAFSDL
     PALVRAVRAA ARPGDHVLVM SNGGFGGVHQ KLLDAFAAGA TA
//
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