ID A0A5C7ETE9_9ACTN Unreviewed; 480 AA. AC A0A5C7ETE9; DT 13-NOV-2019, integrated into UniProtKB/TrEMBL. DT 13-NOV-2019, sequence version 1. DT 03-MAY-2023, entry version 14. DE RecName: Full=UDP-N-acetylmuramate--L-alanine ligase {ECO:0000256|ARBA:ARBA00012211, ECO:0000256|HAMAP-Rule:MF_00046}; DE EC=6.3.2.8 {ECO:0000256|ARBA:ARBA00012211, ECO:0000256|HAMAP-Rule:MF_00046}; DE AltName: Full=UDP-N-acetylmuramoyl-L-alanine synthetase {ECO:0000256|HAMAP-Rule:MF_00046}; GN Name=murC {ECO:0000256|HAMAP-Rule:MF_00046}; GN ORFNames=E4J93_03495 {ECO:0000313|EMBL:TXF37596.1}; OS Collinsella sp. BA40. OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales; OC Coriobacteriaceae; Collinsella. OX NCBI_TaxID=2560852 {ECO:0000313|EMBL:TXF37596.1, ECO:0000313|Proteomes:UP000321063}; RN [1] {ECO:0000313|EMBL:TXF37596.1, ECO:0000313|Proteomes:UP000321063} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BA40 {ECO:0000313|EMBL:TXF37596.1, RC ECO:0000313|Proteomes:UP000321063}; RA Park J.-K.; RT "Collinsella canisensis sp. nov., a novel bacterium isolated from canine RT feces."; RL Submitted (AUG-2019) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00046}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + CC phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; CC Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, CC ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; CC Evidence={ECO:0000256|ARBA:ARBA00001677, ECO:0000256|HAMAP- CC Rule:MF_00046}; CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000256|ARBA:ARBA00004752, ECO:0000256|HAMAP-Rule:MF_00046}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, CC ECO:0000256|HAMAP-Rule:MF_00046}. CC -!- SIMILARITY: Belongs to the MurCDEF family. {ECO:0000256|HAMAP- CC Rule:MF_00046}. 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:TXF37596.1}. 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; VOWY01000007; TXF37596.1; -; Genomic_DNA. DR AlphaFoldDB; A0A5C7ETE9; -. DR OrthoDB; 9804126at2; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000321063; 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:0008763; F:UDP-N-acetylmuramate-L-alanine ligase activity; IEA:UniProtKB-UniRule. 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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR HAMAP; MF_00046; MurC; 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; IPR005758; UDP-N-AcMur_Ala_ligase_MurC. DR PANTHER; PTHR43445:SF3; UDP-N-ACETYLMURAMATE--L-ALANINE LIGASE; 1. DR PANTHER; PTHR43445; UDP-N-ACETYLMURAMATE--L-ALANINE LIGASE-RELATED; 1. DR Pfam; PF01225; Mur_ligase; 1. DR Pfam; PF02875; Mur_ligase_C; 1. DR Pfam; PF08245; Mur_ligase_M; 1. DR SUPFAM; SSF51984; MurCD N-terminal domain; 1. DR SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1. DR SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1. DR TIGRFAMs; TIGR01082; murC; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00046}; KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP- KW Rule:MF_00046}; KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP- KW Rule:MF_00046}; KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP- KW Rule:MF_00046}; KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316, KW ECO:0000256|HAMAP-Rule:MF_00046}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00046}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_00046, ECO:0000313|EMBL:TXF37596.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00046}; KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP- KW Rule:MF_00046}; Reference proteome {ECO:0000313|Proteomes:UP000321063}. FT DOMAIN 19..117 FT /note="Mur ligase N-terminal catalytic" FT /evidence="ECO:0000259|Pfam:PF01225" FT DOMAIN 122..303 FT /note="Mur ligase central" FT /evidence="ECO:0000259|Pfam:PF08245" FT DOMAIN 324..407 FT /note="Mur ligase C-terminal" FT /evidence="ECO:0000259|Pfam:PF02875" FT BINDING 124..130 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00046" SQ SEQUENCE 480 AA; 50887 MW; 3BF0AEBCCD361B08 CRC64; MSNIVVPEST AAPTFASAHF IGVGGAGMSG IALVLHERGY EVTGSDLKTS RYIRQLSRAG MEVFVGHDAA TIDAVKPDVV VVSTAIPETN PELIRARELG IPVWPRAKML SALGAGYTTL AVAGTHGKTT TSSMCATMLD RMGLDPSFLI GGIVEGYDTN GRNGAGEYFV CEADESDSSF LYLDPDVVVV TNVEADHMDH YESLAQIEET FCTFMGLVGD EGTVIACGED PRLVELARST GRAVVTYGLD PSNDVVCTVH PAAHALGSTF DVTLPDGSVR EVSIQHNPGA HNVLNATASL AAAYVMGLDT SAAAEALSTF EGARRRFTHI GDTRGVTVVD DYGHHPTEIK ATLAAAHGLD FNNVVVVFQP HRYSRLQALC DDFANAFADA DKLVLIDVFP AGEMPIPGVT SKMLADTIRT LHPDKDVVYV DDRPALMEHL DALVNEGDLL ITMGAGDVTT VGPDYIEHVA DLERAAGSRA //