ID MUDD_CHLTR Reviewed; 803 AA. AC O84767; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 27-MAR-2024, entry version 149. DE RecName: Full=Bifunctional enzyme MurC/Ddl; DE Includes: DE RecName: Full=UDP-N-acetylmuramate--L-alanine ligase; DE EC=6.3.2.8; DE AltName: Full=UDP-N-acetylmuramoyl-L-alanine synthetase; DE Includes: DE RecName: Full=D-alanine--D-alanine ligase; DE EC=6.3.2.4; DE AltName: Full=D-Ala-D-Ala ligase; DE AltName: Full=D-alanylalanine synthetase; GN Name=murC/ddl; OrderedLocusNames=CT_762; OS Chlamydia trachomatis (strain D/UW-3/Cx). OC Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae; OC Chlamydia/Chlamydophila group; Chlamydia. OX NCBI_TaxID=272561; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=D/UW-3/Cx; RX PubMed=9784136; DOI=10.1126/science.282.5389.754; RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L., RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.; RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia RT trachomatis."; RL Science 282:754-759(1998). CC -!- FUNCTION: Cell wall formation. {ECO:0000250}. 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 -!- CATALYTIC ACTIVITY: CC Reaction=ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + CC phosphate; Xref=Rhea:RHEA:11224, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57416, CC ChEBI:CHEBI:57822, ChEBI:CHEBI:456216; EC=6.3.2.4; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250}; CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: In the N-terminal section; belongs to the MurCDEF family. CC {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the D-alanine--D- CC alanine ligase family. {ECO:0000305}. 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; AE001273; AAC68357.1; -; Genomic_DNA. DR PIR; A71475; A71475. DR RefSeq; NP_220281.1; NC_000117.1. DR RefSeq; WP_010725335.1; NC_000117.1. DR AlphaFoldDB; O84767; -. DR SMR; O84767; -. DR STRING; 272561.CT_762; -. DR EnsemblBacteria; AAC68357; AAC68357; CT_762. DR GeneID; 884562; -. DR KEGG; ctr:CT_762; -. DR PATRIC; fig|272561.5.peg.837; -. DR HOGENOM; CLU_019395_0_0_0; -. DR InParanoid; O84767; -. DR OrthoDB; 9804126at2; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000000431; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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; 3.40.50.20; -; 1. DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1. DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1. 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_00047; Dala_Dala_lig; 1. DR HAMAP; MF_00046; MurC; 1. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR000291; D-Ala_lig_Van_CS. DR InterPro; IPR005905; D_ala_D_ala. DR InterPro; IPR011095; Dala_Dala_lig_C. DR InterPro; IPR011127; Dala_Dala_lig_N. 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; IPR016185; PreATP-grasp_dom_sf. DR InterPro; IPR005758; UDP-N-AcMur_Ala_ligase_MurC. DR NCBIfam; TIGR01205; D_ala_D_alaTIGR; 1. 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; PF07478; Dala_Dala_lig_C; 1. DR Pfam; PF01820; Dala_Dala_lig_N; 1. DR Pfam; PF01225; Mur_ligase; 1. DR Pfam; PF02875; Mur_ligase_C; 1. DR Pfam; PF08245; Mur_ligase_M; 1. DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 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 SUPFAM; SSF52440; PreATP-grasp domain; 1. DR PROSITE; PS50975; ATP_GRASP; 1. DR PROSITE; PS00843; DALA_DALA_LIGASE_1; 1. DR PROSITE; PS00844; DALA_DALA_LIGASE_2; 1. PE 3: Inferred from homology; KW ATP-binding; Cell cycle; Cell division; Cell shape; KW Cell wall biogenesis/degradation; Cytoplasm; Ligase; Magnesium; Manganese; KW Metal-binding; Multifunctional enzyme; Nucleotide-binding; KW Peptidoglycan synthesis; Reference proteome. FT CHAIN 1..803 FT /note="Bifunctional enzyme MurC/Ddl" FT /id="PRO_0000177916" FT DOMAIN 567..778 FT /note="ATP-grasp" FT REGION 1..446 FT /note="UDP-N-acetylmuramate--alanine ligase" FT REGION 447..803 FT /note="D-alanine--D-alanine ligase" FT BINDING 111..117 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255" FT BINDING 600..655 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 732 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 745 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 745 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 747 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250" SQ SEQUENCE 803 AA; 89230 MW; 82BB523BF1F4C1C8 CRC64; MMKSLFYHFI GIGGIGMSAL AHVLLDRGYS VSGSDLSEGK VVEKLKNKGA EFFLGNQEEH IPEGAVVVYS SSISKKNPEF LSAKSRGNRV VHRAELLAEL AQDQISIFVT GSHGKTTVSS LITAILQEAK KNPSFAIGGL NQEGINGGSG SEYFVAEADE SDGSIRCYTP EFSVITNIDD EHLSNFEGDR ELLLASLKDF ALKTQQICWY NGDCPRLRSC LQGHTFGLDS SCDLHILSYY QEGWRLYFTA KYQDVVYADI EVQLVGMHNV LNAAAAMGIA LSLGIDEGAI RNAFRGFSGV QRRLQRKNSS ETFLFLEDYA HHPSEISCTL RAVRTAVGQR RILAIYQPHR FSRLRECIDS FPSAFKDADE VLLTEVYSAG EEAEDISYQK LAEAISQESI VKCTHIPFHE LQRHLEQSIR VHDVCVSLGA GNIVNLGEKL RDFEPQKLHL GIICGGKSCE HEISVLSAKN IAKHLSKSFY DVSYFLITRE GLWESVSSLE TAEDSGKSVF DPEIAQRLEK VDVVLPILHG PYGEDGAMQG FLETIGKPYT GPAIAFSAIA MNKVFTKRFM SDLGIPVVPY LPLTLAGWKQ EQDKWLAHIV EAFSFPIFVK SSHLGSSIGV FEVHNVIELR DAINEAFMRD NDVFVEENRL GCKEIEVSVL GDGSGAFVVA GLHERRGSGG FIDYQEKYGL SGKSSAQIVF DTDLSKEIQE QILEAADKIY RLLLGKGSCR IDFFVDEEGN FWLSEMNPIP GMTETSPFLT SFIRKGWSYE QIVHQLVIDG LQRFNQRQRL ISTSFVDQAF AIQ //