ID A0A926M5G4_9PROT Unreviewed; 464 AA. AC A0A926M5G4; DT 22-FEB-2023, integrated into UniProtKB/TrEMBL. DT 22-FEB-2023, sequence version 1. DT 24-JUL-2024, entry version 6. 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 ECO:0000313|EMBL:MBD1142734.1}; GN ORFNames=IDH22_01980 {ECO:0000313|EMBL:MBD1142734.1}; OS Pelagibacterales bacterium SAG-MED35. OC Bacteria; Pseudomonadota; Alphaproteobacteria; Candidatus Pelagibacterales. OX NCBI_TaxID=2760037 {ECO:0000313|EMBL:MBD1142734.1, ECO:0000313|Proteomes:UP000611396}; RN [1] {ECO:0000313|EMBL:MBD1142734.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SAG-MED35 {ECO:0000313|EMBL:MBD1142734.1}; RX PubMed=31840364; RA Haro-Moreno J.M., Rodriguez-Valera F., Rosselli R., Martinez-Hernandez F., RA Roda-Garcia J.J., Gomez M.L., Fornas O., Martinez-Garcia M., RA Lopez-Perez M.; RT "Ecogenomics of the SAR11 clade."; RL Environ. Microbiol. 22:1748-1763(2020). 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|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:MBD1142734.1}. 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; JACWEF010000008; MBD1142734.1; -; Genomic_DNA. DR Proteomes; UP000611396; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. 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: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; IPR050061; MurCDEF_pg_biosynth. DR InterPro; IPR005758; UDP-N-AcMur_Ala_ligase_MurC. DR NCBIfam; TIGR01082; murC; 1. 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. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW 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|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00046}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00046}; KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP- KW Rule:MF_00046}; Reference proteome {ECO:0000313|Proteomes:UP000611396}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 10..28 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 11..105 FT /note="Mur ligase N-terminal catalytic" FT /evidence="ECO:0000259|Pfam:PF01225" FT DOMAIN 113..298 FT /note="Mur ligase central" FT /evidence="ECO:0000259|Pfam:PF08245" FT DOMAIN 318..400 FT /note="Mur ligase C-terminal" FT /evidence="ECO:0000259|Pfam:PF02875" FT BINDING 115..121 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00046" SQ SEQUENCE 464 AA; 52708 MW; 4FDA6B44445916C8 CRC64; MKIKLAKTEL IHFIGIGGIG MSGLALIMKG KGFRVQGSDI SINKNIERLK KEKIKILIGH KKQNINKATI LVVSSAIKKN NPEMLEAIKR QLPIYKRGEM LANTVSLTKN IVVVGSHGKT TTTSLIASIF QETKIDPTII NGGVINSLNN SAKLGKSEWS ILEADESDGS FVHTPPTYAI ITNIDREHMD YYGSMEKLNK YFVNFVNKVP SFGKSFICLD NKNNKNLLKK LKNKNFYTYG IDNKSNYIVK NIKQFREYSE YDLKIRLPNK KIVIIRKIKI PLLGLHNIKN SVAATAVALN VGLSISNIKK GLKNFKGVQR RFNKIFTFNK VDFFDDYAHH PTEIKEVLNG VKKVYSNYEK ICIFQPHRIS RLKDLKSEFA SAFKDADKVI LFPIYTAGEK IKLGFSYYSF AKEIIKKSKV ELFLVNDKYQ LAKYIKYNIY GDKIVIGMGA GSISSWMREM PKFL //