ID C5QLA9_9STAP Unreviewed; 451 AA. AC C5QLA9; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 22-FEB-2023, entry version 74. 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 ECO:0000313|EMBL:EES42326.1}; GN ORFNames=HMPREF0793_0015 {ECO:0000313|EMBL:EES42326.1}; OS Staphylococcus caprae M23864:W1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=525378 {ECO:0000313|EMBL:EES42326.1, ECO:0000313|Proteomes:UP000003152}; RN [1] {ECO:0000313|EMBL:EES42326.1, ECO:0000313|Proteomes:UP000003152} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M23864:W1 {ECO:0000313|EMBL:EES42326.1, RC ECO:0000313|Proteomes:UP000003152}; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L., RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G., RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L., RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A., RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R., RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R., RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P., RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y., RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L., RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.; RL Submitted (JAN-2009) 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:EES42326.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; ACJB01000001; EES42326.1; -; Genomic_DNA. DR RefSeq; WP_002445538.1; NZ_GG696776.1. DR AlphaFoldDB; C5QLA9; -. DR STRING; 525378.HMPREF0793_0015; -. DR EnsemblBacteria; EES42326; EES42326; HMPREF0793_0015. DR GeneID; 58050646; -. DR eggNOG; COG0770; Bacteria. DR HOGENOM; CLU_031507_1_0_9; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000003152; 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; IPR000713; Mur_ligase_N. DR InterPro; IPR035911; MurE/MurF_N. DR InterPro; IPR005863; UDP-N-AcMur_synth. 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. DR TIGRFAMs; TIGR01143; murF; 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:EES42326.1}; 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 26..100 FT /note="Mur ligase N-terminal catalytic" FT /evidence="ECO:0000259|Pfam:PF01225" FT DOMAIN 111..294 FT /note="Mur ligase central" FT /evidence="ECO:0000259|Pfam:PF08245" FT DOMAIN 317..392 FT /note="Mur ligase C-terminal" FT /evidence="ECO:0000259|Pfam:PF02875" FT BINDING 113..119 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02019" SQ SEQUENCE 451 AA; 49744 MW; 1D88E5B68457B276 CRC64; MINVTLQQIQ NWISCEIDEQ YLSRSIKGVT IDSRAIEKDM LFIPFKGENV DGHRFIDQAL KDGAVASFSE KGTELSEDVE GPIIWVEDTL QALQDLAKAY LKHVNPKVIA VTGSNGKTTT KDMIESVLTT EFKVKKTQGN YNNEIGMPLT ILDLDEDTEI SILEMGMSGF HEIELLSTIA EPDIAVITNI GESHMQDLGS REGIAKAKSE ITIGLKDNGT FIYDGDEPLL TPHVKQIQQA KLISVGLGDA NSLVCHVDDV ETEGIGFTIN NDESYVLPIL GIHNMKNAAI AIAVGHELGL PYATIKENIR HVQLTGMRME RHQTDDNVTV INDAYNASPT SMKAAIDTLS SMEGRKILIL ADVLELGTNS QQMHEEVGTY LDGKSIDILF TYGTEAEYIF NTGQSYVETA KHFDDKSELI KELKAIVKEN DKILVKGSRG MKLEEVVEAL I //