ID MUDD_CHLPN Reviewed; 809 AA.
AC Q9Z701; Q9JQB5;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 24-JAN-2024, entry version 173.
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=CPn_0905, CP_0961, CpB0937;
OS Chlamydia pneumoniae (Chlamydophila pneumoniae).
OC Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=83558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CWL029;
RX PubMed=10192388; DOI=10.1038/7716;
RA Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W.,
RA Olinger L., Grimwood J., Davis R.W., Stephens R.S.;
RT "Comparative genomes of Chlamydia pneumoniae and C. trachomatis.";
RL Nat. Genet. 21:385-389(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR39;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J138;
RX PubMed=10871362; DOI=10.1093/nar/28.12.2311;
RA Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K.,
RA Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.;
RT "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from
RT Japan and CWL029 from USA.";
RL Nucleic Acids Res. 28:2311-2314(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW-183;
RA Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P.,
RA Schneider S., Pohl T., Essig A., Marre R., Melchers K.;
RT "The genome sequence of Chlamydia pneumoniae TW183 and comparison with
RT other Chlamydia strains based on whole genome sequence analysis.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; AE001363; AAD19043.1; -; Genomic_DNA.
DR EMBL; AE002161; AAF38741.1; -; Genomic_DNA.
DR EMBL; BA000008; BAA99113.1; -; Genomic_DNA.
DR EMBL; AE009440; AAP98866.1; -; Genomic_DNA.
DR PIR; D72022; D72022.
DR PIR; G86603; G86603.
DR RefSeq; NP_225100.1; NC_000922.1.
DR RefSeq; WP_010883540.1; NZ_LN847257.1.
DR AlphaFoldDB; Q9Z701; -.
DR SMR; Q9Z701; -.
DR STRING; 406984.CPK_ORF00317; -.
DR GeneID; 45050961; -.
DR KEGG; cpa:CP_0961; -.
DR KEGG; cpj:murC_ddlA; -.
DR KEGG; cpn:CPn_0905; -.
DR KEGG; cpt:CpB0937; -.
DR PATRIC; fig|115713.3.peg.986; -.
DR eggNOG; COG0773; Bacteria.
DR eggNOG; COG1181; Bacteria.
DR HOGENOM; CLU_019395_0_0_0; -.
DR OrthoDB; 9804126at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000583; Chromosome.
DR Proteomes; UP000000801; 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..809
FT /note="Bifunctional enzyme MurC/Ddl"
FT /id="PRO_0000177915"
FT DOMAIN 573..784
FT /note="ATP-grasp"
FT REGION 1..450
FT /note="UDP-N-acetylmuramate--alanine ligase"
FT REGION 451..809
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 606..661
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 738
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 751
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 751
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 753
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CONFLICT 560
FT /note="L -> P (in Ref. 4; AAP98866)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 809 AA; 89964 MW; 1A204C6B20E03B47 CRC64;
MKGTPQYHFI GIGGIGMSAL AHILLDRGYE VSGSDLYESY TIESLKAKGA RCFSGHDSSH
VPHDAVVVYS SSIAPDNVEY LTAIQRSSRL LHRAELLSQL MEGYESILVS GSHGKTGTSS
LIRAIFQEAQ KDPSYAIGGL AANCLNGYSG SSKIFVAEAD ESDGSLKHYT PRAVVITNID
NEHLNNYAGN LDNLVQVIQD FSRKVTDLNK VFYNGDCPIL KGNVQGISYG YSPECQLHIV
SYNQKAWQSH FSFTFLGQEY QDIELNLPGQ HNAANAAAAC GVALTFGIDI NIIRKALKKF
SGVHRRLERK NISESFLFLE DYAHHPVEVA HTLRSVRDAV GLRRVIAIFQ PHRFSRLEEC
LQTFPKAFQE ADEVILTDVY SAGESPRESI ILSDLAEQIR KSSYVHCCYV PHGDIVDYLR
NYIRIHDVCV SLGAGNIYTI GEALKDFNPK KLSIGLVCGG KSCEHDISLL SAQHVSKYIS
PEFYDVSYFI INRQGLWRTG KDFPHLIEET QGDSPLSSEI ASALAKVDCL FPVLHGPFGE
DGTIQGFFEI LGKPYAGPSL SLAATAMDKL LTKRIASAVG VPVVPYQPLN LCFWKRNPEL
CIQNLIETFS FPMIVKTAHL GSSIGIFLVR DKEELQEKIS EAFLYDTDVF VEESRLGSRE
IEVSCIGHSS SWYCMAGPNE RCGASGFIDY QEKYGFDGID CAKISFDLQL SQESLDCVRE
LAERVYRAMQ GKGSARIDFF LDEEGNYWLS EVNPIPGMTA ASPFLQAFVH AGWTQEQIVD
HFIIDALHKF DKQQTIEQAF TKEQDLVKR
//
