ID MUDD_CHLMU Reviewed; 802 AA. AC Q9PLG1; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 2. DT 24-JAN-2024, entry version 146. 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=TC_0143; OS Chlamydia muridarum (strain MoPn / Nigg). OC Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae; OC Chlamydia/Chlamydophila group; Chlamydia. OX NCBI_TaxID=243161; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MoPn / Nigg; RX PubMed=10684935; DOI=10.1093/nar/28.6.1397; RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O., RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S., RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J., RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G., RA Salzberg S.L., Eisen J.A., Fraser C.M.; RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae RT AR39."; RL Nucleic Acids Res. 28:1397-1406(2000). 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 -!- SEQUENCE CAUTION: CC Sequence=AAF39021.1; Type=Erroneous initiation; Evidence={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; AE002160; AAF39021.1; ALT_INIT; Genomic_DNA. DR PIR; B81737; B81737. DR RefSeq; WP_010229511.1; NZ_CP027217.1. DR AlphaFoldDB; Q9PLG1; -. DR SMR; Q9PLG1; -. DR GeneID; 1245677; -. DR KEGG; cmu:TC_0143; -. DR eggNOG; COG0773; Bacteria. DR eggNOG; COG1181; Bacteria. DR HOGENOM; CLU_019395_0_0_0; -. DR OrthoDB; 9804126at2; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000000800; 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. FT CHAIN 1..802 FT /note="Bifunctional enzyme MurC/Ddl" FT /id="PRO_0000177914" FT DOMAIN 566..777 FT /note="ATP-grasp" FT REGION 1..445 FT /note="UDP-N-acetylmuramate--alanine ligase" FT REGION 446..802 FT /note="D-alanine--D-alanine ligase" FT BINDING 110..116 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255" FT BINDING 599..654 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 731 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 744 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 744 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 746 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250" SQ SEQUENCE 802 AA; 88744 MW; 3FAF071C3CB78F96 CRC64; MKSLCYHFIG IGGIGMSALA HILLDRGYSV SGSDLSEGKI VETLKNKGVK FFLGNQEEHV PEESVVVYGS GISKNNPEFL AALNKGNRLI HRAELLAELT KEQISIFVTG SHGKTTVSSL ITVILQEAGK TPSFAIGGLN GEGINGSSGS EYFVAEADES DGSIRNYSPE FSVITNIDDE HLSNFGGDRE RLLASLQDFS TKTRQICWYN GDCSRLRSCL VGHTFGFTSS CDLHILTYRQ EGWRSFFTVR YQNVLYEDVE VRLVGEHNVM NAAAAMGVAL SLGIDEDTIR DALQRFPGVQ RRLQRKNSSE VFLFLEDYAH HPSEIACTLQ AVRSAVGSRR VLAICQPHRF SRLKECMGCF PSAFKGADEV LLTDVYSAGE AEEDVSYKEL AQSISRESLV TCAYVPFSEL QGFLEKHIRV HDVCVALGAG DIEVLGESLR DFEPKKLSLG LICGGRSCEH DISILSAQNI AKYLSHSFYE VQYFLITREG LWKTGSSLEL SEETGKTIFD PEIAGKLSKV DVILPILHGP YGEDGAMQGF LETIGKPYTG PSLVFAAIGM NKVLTKRFMS DLGIPVVPYL PLTLKGWKQD QEKCLAQIKA AFSFPMFVKS VHLGSSIGVF EVHDTNELRD AINEAFVRDD DVFIEESRLG CREIEVSFLG DGSGVFFVAG MHERRGRGGF IDYQEKYGLS GRASAQIVFD VDLSKETREQ LLGVAEKIYR LLQGKGSCRI DFFVDNEGSF WLSEINPIPG MTTASPFLAA FVRKGWNREQ IVHQLVIDGL QRFDQRQRLI STPLIDQALA AR //