ID A0A291GYM1_9MICO Unreviewed; 490 AA.
AC A0A291GYM1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=CFK41_11510 {ECO:0000313|EMBL:ATG55321.1};
OS Brachybacterium ginsengisoli.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC Brachybacterium.
OX NCBI_TaxID=1331682 {ECO:0000313|EMBL:ATG55321.1, ECO:0000313|Proteomes:UP000217889};
RN [1] {ECO:0000313|EMBL:ATG55321.1, ECO:0000313|Proteomes:UP000217889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DCY80 {ECO:0000313|EMBL:ATG55321.1,
RC ECO:0000313|Proteomes:UP000217889};
RX PubMed=24944333; DOI=10.1099/ijs.0.058388-0;
RA Hoang V.A., Kim Y.J., Nguyen N.L., Yang D.C.;
RT "Brachybacterium ginsengisoli sp. nov., isolated from soil of a ginseng
RT field.";
RL Int. J. Syst. Evol. Microbiol. 64:3063-3068(2014).
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02019}.
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DR EMBL; CP023564; ATG55321.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A291GYM1; -.
DR KEGG; bgg:CFK41_11510; -.
DR OrthoDB; 9800958at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000217889; 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:ATG55321.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02019};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP-
KW Rule:MF_02019}.
FT DOMAIN 32..95
FT /note="Mur ligase N-terminal catalytic"
FT /evidence="ECO:0000259|Pfam:PF01225"
FT DOMAIN 112..310
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 333..414
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 490 AA; 50626 MW; 8BD2447DB70E8847 CRC64;
MLQTTARDIA ALTGGDLVGG ASGDELVTGI AQIDSREVST GDLFAAFRGE RVDGHEFLDA
AHRAGAALSL VTEDRGVPAV RVADVREALS QLAHAQLDRA REENPQLVVL AVTGSAGKTG
TKDLLGAILR ASGPVVAPVG SLNNELGLPL TVLRLDAETR YLVLEMGARG IGHIAQLTAI
ARPDISLVLN VGSAHLGEFG GVEATARAKG ELVEALAPTG RAVLNAEDRL VAAMAERSEA
PVVTWGFTTG DVRGGDLSLD DQARVSFSLE VPAGLTTLSG ASVPAGDFPV RTDLLGEHQA
SNVLAALTAA LVAGVDPSAA AAALEGATLA SGQRMQALHA GGALIIDDAY NANPDSMRQA
LKTLAHLGRS HRTIAVLGEM LELGPDTVRL HDEIGRLAVR LNIGQLYVVG DGAAAIHHGA
SLEGSFGGES EYLDTVEDAI DLLQRTVRPG DAVLLKSSRD AGLRRIAGPL VEQLELRGDS
EEPDLTGADR
//
