ID A0A0G1CCK7_9BACT Unreviewed; 416 AA.
AC A0A0G1CCK7;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase {ECO:0000256|RuleBase:RU004136};
DE EC=6.3.2.10 {ECO:0000256|RuleBase:RU004136};
GN ORFNames=UV20_C0012G0007 {ECO:0000313|EMBL:KKS56431.1};
OS Candidatus Magasanikbacteria bacterium GW2011_GWA2_42_32.
OC Bacteria; Candidatus Magasanikbacteria.
OX NCBI_TaxID=1619039 {ECO:0000313|EMBL:KKS56431.1, ECO:0000313|Proteomes:UP000034837};
RN [1] {ECO:0000313|EMBL:KKS56431.1, ECO:0000313|Proteomes:UP000034837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
CC -!- FUNCTION: Involved in cell wall formation. Catalyzes the final step in
CC the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of
CC murein. {ECO:0000256|RuleBase:RU004136}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-muramoyl-L-
CC alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate = ADP + H(+) +
CC phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-
CC meso-2,6-diaminopimeloyl-D-alanyl-D-alanine; Xref=Rhea:RHEA:28374,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57822, ChEBI:CHEBI:61386, ChEBI:CHEBI:83905,
CC ChEBI:CHEBI:456216; EC=6.3.2.10;
CC Evidence={ECO:0000256|RuleBase:RU004136};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|RuleBase:RU004136}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU004136}.
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:KKS56431.1}.
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DR EMBL; LCDO01000012; KKS56431.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1CCK7; -.
DR PATRIC; fig|1619039.3.peg.1036; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000034837; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0047480; F:UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0008766; F:UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate-D-alanyl-D-alanine 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-UniPathway.
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 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; IPR005863; UDP-N-AcMur_synth.
DR NCBIfam; TIGR01143; murF; 1.
DR PANTHER; PTHR43024; UDP-N-ACETYLMURAMOYL-TRIPEPTIDE--D-ALANYL-D-ALANINE LIGASE; 1.
DR PANTHER; PTHR43024:SF1; UDP-N-ACETYLMURAMOYL-TRIPEPTIDE--D-ALANYL-D-ALANINE LIGASE; 1.
DR Pfam; PF02875; Mur_ligase_C; 1.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
PE 4: Predicted;
KW Cell cycle {ECO:0000256|RuleBase:RU004136};
KW Cell division {ECO:0000256|RuleBase:RU004136};
KW Cell shape {ECO:0000256|RuleBase:RU004136};
KW Cell wall biogenesis/degradation {ECO:0000256|RuleBase:RU004136};
KW Ligase {ECO:0000313|EMBL:KKS56431.1};
KW Peptidoglycan synthesis {ECO:0000256|RuleBase:RU004136}.
FT DOMAIN 73..255
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 278..354
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 416 AA; 46688 MW; 3151CC74C62AA329 CRC64;
MKSKRVPSLI QWWFGPGLSV EYIFISKDRR PQNTYKLIRL YFRTWLIHPI KRRIAKLYVL
LLQKLFGLTV IAITGSAGKT STKDMIASIL NQKNRTVFSH ANITPTFNIP TTILQCTRKT
KYLVLEMGVE YPGDMDFYLW LVKPNVGIIT NIYQTHTEYF KDVEGVSREK TKLVKALDSN
DFVILNKENE HLKSIASKLK SQLVWFGERG EVSASDEKVS SDGTSFTLQI GHTKEEIHLS
FIGKQFVSNS LAAVAGAYAI GATVQEIKGG LEKLKPAEHR MNLLYLKSGA VILDDTYNSN
PSAAKKALET LREISGKKQT VAVLGDMLEL GENEKEIHKE LGKYCSSLGI NYVLGVGNLA
QNVVGEFYKK SEVSKYWVPK AENSYDLLKP FLKKDVVVLI KGSRSIGLDK LVAKLA
//
