ID A0A1D8T5G4_9NOCA Unreviewed; 504 AA.
AC A0A1D8T5G4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase {ECO:0000256|HAMAP-Rule:MF_02019, ECO:0000256|RuleBase:RU004136};
DE EC=6.3.2.10 {ECO:0000256|HAMAP-Rule:MF_02019, ECO:0000256|RuleBase:RU004136};
DE AltName: Full=D-alanyl-D-alanine-adding enzyme {ECO:0000256|HAMAP-Rule:MF_02019};
GN Name=murF {ECO:0000256|HAMAP-Rule:MF_02019};
GN ORFNames=BFN03_09525 {ECO:0000313|EMBL:AOW92837.1};
OS Rhodococcus sp. WMMA185.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=679318 {ECO:0000313|EMBL:AOW92837.1, ECO:0000313|Proteomes:UP000178767};
RN [1] {ECO:0000313|EMBL:AOW92837.1, ECO:0000313|Proteomes:UP000178767}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WMMA185 {ECO:0000313|EMBL:AOW92837.1,
RC ECO:0000313|Proteomes:UP000178767};
RA Bugni T.S., Adnani N., Braun D., Chevrette M., McDonald B., Rajski S.;
RT "Draft Genome of Rhodococcus sp. WMMA185.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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|HAMAP-Rule:MF_02019,
CC 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; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_02019, ECO:0000256|RuleBase:RU004136};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_02019, ECO:0000256|RuleBase:RU004136}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02019,
CC ECO:0000256|RuleBase:RU004136}.
CC -!- SIMILARITY: Belongs to the MurCDEF family. MurF subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_02019}.
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DR EMBL; CP017014; AOW92837.1; -; Genomic_DNA.
DR RefSeq; WP_070378814.1; NZ_CP017014.1.
DR AlphaFoldDB; A0A1D8T5G4; -.
DR STRING; 679318.BFN03_09525; -.
DR KEGG; rhw:BFN03_09525; -.
DR OrthoDB; 9800958at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000178767; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0047480; F:UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase activity; IEA:UniProtKB-UniRule.
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-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; 3.40.1390.10; MurE/MurF, N-terminal domain; 1.
DR HAMAP; MF_02019; MurF; 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; IPR000713; Mur_ligase_N.
DR InterPro; IPR035911; MurE/MurF_N.
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; PF01225; Mur_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.
DR SUPFAM; SSF63418; MurE/MurF N-terminal domain; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_02019};
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW Rule:MF_02019};
KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW Rule:MF_02019};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW Rule:MF_02019};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW ECO:0000256|HAMAP-Rule:MF_02019};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02019};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_02019, ECO:0000313|EMBL:AOW92837.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02019};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP-
KW Rule:MF_02019}; Reference proteome {ECO:0000313|Proteomes:UP000178767}.
FT DOMAIN 31..77
FT /note="Mur ligase N-terminal catalytic"
FT /evidence="ECO:0000259|Pfam:PF01225"
FT DOMAIN 132..322
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 344..429
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
FT BINDING 134..140
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02019"
SQ SEQUENCE 504 AA; 51364 MW; C25CAB9783F93B68 CRC64;
MIPMTLARIA QIVGGELHDV DDPCVEVTGT VEFDSREIAD GGLFLALPGA RVDGHDHSAA
AIEAGAVAVL AARPVGVPAI VLPPKPGDVP SRAMALEHDA DGSGAAVLGA LASLARASVD
GLAANGLTVV GVTGSAGKTS TKDLLAALLR PLGPVVAPPG SFNNELGHPW TALRADADTR
FLVLEMSARG RGHISALADI ATPKIGVVLN VGTAHLGEFG SRDAIAAAKG ELVESLPSAA
DGGVAILNAD DPLVAAMATR TSARVVLVGQ SETADVRATD VTLDEKARAR FTLTTPAGSV
PVSLVVHGEH QVGNALAAAA VALECGADLE QIARVLGGAS AVSARRMDVR DRPDGVTVIN
DSYNANPDSM RAAIKALVSM ARTGRGQARR SWAVLGEMAE LGPESVVEHD AIGRFAVRLD
VSRLIVVGTG RPSRAMHQGA VMEGSWGEES ILVPDIAGAV AVLEEQLQPG DLVLVKASKS
IGLWEVADAV LAETTGPKGS EAEQ
//
