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Database: UniProt
Entry: A0A1T1AX76_RHOFE
LinkDB: A0A1T1AX76_RHOFE
Original site: A0A1T1AX76_RHOFE 
ID   A0A1T1AX76_RHOFE        Unreviewed;       467 AA.
AC   A0A1T1AX76;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
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=RF819_20025 {ECO:0000313|EMBL:OOV08681.1};
OS   Rhodoferax fermentans.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Rhodoferax.
OX   NCBI_TaxID=28066 {ECO:0000313|EMBL:OOV08681.1, ECO:0000313|Proteomes:UP000190750};
RN   [1] {ECO:0000313|EMBL:OOV08681.1, ECO:0000313|Proteomes:UP000190750}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 7819 {ECO:0000313|EMBL:OOV08681.1,
RC   ECO:0000313|Proteomes:UP000190750};
RA   Kim Y.J., Farh M.E.-A., Yang D.-C.;
RT   "Genome sequencing of Rhodoferax fermentans JCM 7819.";
RL   Submitted (JAN-2017) 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:OOV08681.1}.
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DR   EMBL; MTJN01000002; OOV08681.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T1AX76; -.
DR   STRING; 28066.RF819_20025; -.
DR   OrthoDB; 9804126at2; -.
DR   UniPathway; UPA00544; -.
DR   Proteomes; UP000190750; 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:UP000190750}.
FT   DOMAIN          2..108
FT                   /note="Mur ligase N-terminal catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01225"
FT   DOMAIN          116..302
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          322..375
FT                   /note="Mur ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02875"
FT   BINDING         118..124
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02020"
SQ   SEQUENCE   467 AA;  49608 MW;  BFD4CB21D1219EDF CRC64;
     MHIHILGICG TFMGGLAALA REAGHRVTGC DAGVYPPMSD QLRALGIELI EGFGAEQLSL
     QPDLFVVGNV VSRARLGDGT PKFPLMEAIL DAGLPYTSGP QWLSEHILQG RHVVAIAGTH
     GKTTTTAMTT WILEQAGLMP GFLVGGVPLN FGVSARLGQG KAFVIEADEY DTAFFDKRSK
     FVHYRPRTAV LNNLEFDHAD IFENLAAIER QFHHLVRTVP GTGAHGSGRV VVNGLEESLA
     RVLHQGCWSE VRSFGAAVSD FAAAGPAHDF DVLHQGRVVG HVSWGLTGVH NQLNALAAIA
     AAEHLGVAPD TAATALGSFE NVKRRMEVRG TVSVGDAGKV TVYDDFAHHP TAIRTTLDGL
     RSSLSPGERI LAMFEPRSNT MKLGTMKALL PWSLESADLS FCHSAGLGWD AAGALAPMGD
     KVLVSDQLDE LVSAVARVAR AGDHIVCMSN GGFGGVHTKL LKALQEK
//
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