MUDD_CHLTR
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 03-AUG-2022, entry version 142.
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; Chlamydiae; 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}.
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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; 813.O172_04250; -.
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 OMA; INRQGLW; -.
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; 3.30.1490.20; -; 1.
DR Gene3D; 3.40.1190.10; -; 1.
DR Gene3D; 3.90.190.20; -; 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 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; SSF52440; SSF52440; 1.
DR SUPFAM; SSF53244; SSF53244; 1.
DR SUPFAM; SSF53623; SSF53623; 1.
DR TIGRFAMs; TIGR01205; D_ala_D_alaTIGR; 1.
DR TIGRFAMs; TIGR01082; murC; 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
