ID A0A429ZQV1_9ENTE Unreviewed; 461 AA.
AC A0A429ZQV1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=CBF35_06695 {ECO:0000313|EMBL:RST96082.1};
OS Vagococcus salmoninarum.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae; Vagococcus.
OX NCBI_TaxID=2739 {ECO:0000313|EMBL:RST96082.1, ECO:0000313|Proteomes:UP000287239};
RN [1] {ECO:0000313|EMBL:RST96082.1, ECO:0000313|Proteomes:UP000287239}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCFB 2777 {ECO:0000313|EMBL:RST96082.1,
RC ECO:0000313|Proteomes:UP000287239};
RA Gulvik C.A.;
RT "Vagococcus spp. assemblies.";
RL Submitted (MAY-2017) 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-L-lysine = ADP + H(+) + phosphate + UDP-N-
CC acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-
CC alanine; Xref=Rhea:RHEA:16085, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57822, ChEBI:CHEBI:70758,
CC ChEBI:CHEBI:83903, ChEBI:CHEBI:456216; EC=6.3.2.10;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02019};
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|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: 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:RST96082.1}.
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DR EMBL; NGJU01000008; RST96082.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A429ZQV1; -.
DR OrthoDB; 9801978at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000287239; Unassembled WGS sequence.
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; 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; 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|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_02019};
KW Cell cycle {ECO:0000256|HAMAP-Rule:MF_02019,
KW ECO:0000256|RuleBase:RU004136};
KW Cell division {ECO:0000256|HAMAP-Rule:MF_02019,
KW ECO:0000256|RuleBase:RU004136};
KW Cell shape {ECO:0000256|HAMAP-Rule:MF_02019,
KW ECO:0000256|RuleBase:RU004136};
KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_02019,
KW ECO:0000256|RuleBase:RU004136};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02019};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_02019, ECO:0000313|EMBL:RST96082.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02019};
KW Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_02019,
KW ECO:0000256|RuleBase:RU004136};
KW Reference proteome {ECO:0000313|Proteomes:UP000287239}.
FT DOMAIN 110..294
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 316..384
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
FT BINDING 112..118
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02019"
SQ SEQUENCE 461 AA; 50544 MW; 920821498DB1ACFD CRC64;
MKLLVSELAK VVKAENDWQQ WADVVVEHVE FDTRKIVKNS LFVPLQGGNR DGHEFLEVAI
ESGASVSLWQ KEVAPARANF PILVVEDTLI AMQKIAMYFL SVVQPKVIGI TGSNGKTTTK
DMVASVLGQQ FETYKTQGNY NNHIGLPYTI LSMPMTTEML VLEMGMDHFG EIEVLSQIAQ
PDVAAITMIG ESHMEFLGSR AGIAKAKMEI VSGLKAGGLL VVPGEEPLLK PLLEQVSQKV
LTFGPSQKNN LSAQITAETK VETTFNVPNY QNSQFVIPVL GQYNVNNALI ALAIGSYFEM
EIGKMATGLA ELDLTKSRTE WLVAANGAEI LSDVYNANPT AMSLVLDTFS QLPSSGRKYA
VLADMGELGD SSQSLHEKMA EHLDPEKIQE VFLFGPQMKA LFKKLSLKYP KGQVSHYDLD
AKGELITKVL EGLQSTDMIV LKGSNSMKLI EIVEKLTENK S
//
