ID A0A1U9K9L1_9BACL Unreviewed; 403 AA.
AC A0A1U9K9L1;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=B0W44_14395 {ECO:0000313|EMBL:AQS56757.1};
OS Novibacillus thermophilus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Thermoactinomycetaceae;
OC Novibacillus.
OX NCBI_TaxID=1471761 {ECO:0000313|EMBL:AQS56757.1, ECO:0000313|Proteomes:UP000188603};
RN [1] {ECO:0000313|EMBL:AQS56757.1, ECO:0000313|Proteomes:UP000188603}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG-1 {ECO:0000313|EMBL:AQS56757.1,
RC ECO:0000313|Proteomes:UP000188603};
RX PubMed=25951858; DOI=10.1099/ijs.0.000306;
RA Yang G., Chen J., Zhou S.;
RT "Novibacillus thermophilus gen. nov., sp. nov., a Gram-staining-negative
RT and moderately thermophilic member of the family Thermoactinomycetaceae.";
RL Int. J. Syst. Evol. Microbiol. 65:2591-2597(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}.
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DR EMBL; CP019699; AQS56757.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1U9K9L1; -.
DR STRING; 1471761.B0W44_14395; -.
DR KEGG; ntr:B0W44_14395; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000188603; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 Peptidoglycan synthesis {ECO:0000256|RuleBase:RU004136};
KW Reference proteome {ECO:0000313|Proteomes:UP000188603}.
FT DOMAIN 54..240
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 263..343
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 403 AA; 44811 MW; 14493BCFAE409437 CRC64;
MKQVRPLAVV IPSRYRHLSF PAETAVIQVS DPYRSFWRLG LWNFRQYPVK TVAITGSAGK
STTTSMVASV LKRRYPIVKT EGNLNTASFL PTYLCRLSSK HRVLLLEMGM KSLGNIAKQC
RVVRPQVGAV TNVGEAHYGS VGGAHNIVKA KQELIDGMRD GGVVWLNADN DRSRKLRTEH
VNVSRYWFGI DQPAHVQGSH IRYTSRGMSF HVHVNGRTYS FTIPAFGKHN VYNALAAIGI
CYAMGFSMAE IQKGLSMFKQ PHMRLQLVKG VRGTLLINDA WNANPTSMIA GLNVLNALSG
NRKSIAVLGD MKELGSYTQQ AYNRVGDYIA RHPVDQLVTV GRYANLIARR AVSKGFNPQK
AVSFRTREAA LRHLLRAPSG SVIYFKASRS LHFEKLVKQL KAG
//
