MUDD_CHLMU
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 03-AUG-2022, entry version 140.
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; Chlamydiae; 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};
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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 STRING; 243161.TC_0143; -.
DR EnsemblBacteria; AAF39021; AAF39021; TC_0143.
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; 307881at2; -.
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; 3.30.1490.20; -; 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.
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
