MUDD_CHLCV
ID MUDD_CHLCV Reviewed; 811 AA.
AC Q821S4;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 127.
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/ddlA; OrderedLocusNames=CCA_00863;
OS Chlamydia caviae (strain ATCC VR-813 / DSM 19441 / 03DC25 / GPIC)
OS (Chlamydophila caviae).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=227941;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-813 / DSM 19441 / 03DC25 / GPIC;
RX PubMed=12682364; DOI=10.1093/nar/gkg321;
RA Read T.D., Myers G.S.A., Brunham R.C., Nelson W.C., Paulsen I.T.,
RA Heidelberg J.F., Holtzapple E.K., Khouri H.M., Federova N.B., Carty H.A.,
RA Umayam L.A., Haft D.H., Peterson J.D., Beanan M.J., White O.,
RA Salzberg S.L., Hsia R.-C., McClarty G., Rank R.G., Bavoil P.M.,
RA Fraser C.M.;
RT "Genome sequence of Chlamydophila caviae (Chlamydia psittaci GPIC):
RT examining the role of niche-specific genes in the evolution of the
RT Chlamydiaceae.";
RL Nucleic Acids Res. 31:2134-2147(2003).
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; AE015925; AAP05604.1; -; Genomic_DNA.
DR RefSeq; WP_011006818.1; NC_003361.3.
DR AlphaFoldDB; Q821S4; -.
DR SMR; Q821S4; -.
DR STRING; 227941.CCA_00863; -.
DR EnsemblBacteria; AAP05604; AAP05604; CCA_00863.
DR KEGG; cca:CCA_00863; -.
DR eggNOG; COG0773; Bacteria.
DR eggNOG; COG1181; Bacteria.
DR HOGENOM; CLU_019395_0_0_0; -.
DR OMA; INRQGLW; -.
DR OrthoDB; 307881at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000002193; 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..811
FT /note="Bifunctional enzyme MurC/Ddl"
FT /id="PRO_0000177913"
FT DOMAIN 574..785
FT /note="ATP-grasp"
FT REGION 1..450
FT /note="UDP-N-acetylmuramate--alanine ligase"
FT REGION 451..811
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 607..662
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 739
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 752
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 752
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 754
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 811 AA; 90491 MW; 096AC84D620947F2 CRC64;
MNRKNHYHFI GIGGIGMSAL AHILLDRGYS VSGSDLNQGI TIDKLIAKGA AYLPGHKESY
VPEEGTIIYG SGIAKDNVEY KEALRKQLPL VHRAELLALL MQEQTSILVS GSHGKTTVSS
LITAIFQTAK KDPSYAIGGL NSQYLNGYSG SSEYFIAEAD ESDGSLKHYF PKVAVVTNLD
NEHLSNFEGS KEKLAQTIEE FTRKVDDPNL CFYNGDCQEL KGRISGISYG FSQECALYIY
SHRQEGWRSV FSLSFLGKDY LDIDLNLIGK HNVANAAAAI GVALTFGIDE ESIREALKSF
SGVQRRMERK NTSEKFLFLE DYAHHPSEIS CTLRALRDAV GLRRIIAICQ PHRFSRLLYC
LEEFFNAFQD ADEVILTDVY SAGEMPLDLP SPEKLAETIS LSSHVCCTYV PYDNVIEHLK
QNIRVHDVCI SLGAGNIHTV GNALKDFEPK KLSVGVVCGG QSCEHDVSLL SARNVVQYLS
PQHYDVQYFV INRQGLWSQV ANLDAGSDYN SKNYHVLSSK IAEALANLDF VLPILHGPFG
EDGTLQGFLE IANKPYGGPS LLFSAISMDK IMTKRLAASV GVPVVPYQPL TLPTWKRTPE
LCMRRILETF TFPMFVKTAH LGSSIGVFEV HNETELKAKI SEAFLYDTDV FIEESRLGSR
EIEVSCLGDA CSCYYISEPH ERRGSKGFIG YEEKYGFNGK SSATIQYDLN LSEESKTRVK
ELTERVYRVI QGKGSCRIDF FLDREGNFWL SEMNPIPGMT KSSPFLHDFA RLGWTFEQIV
HQLIIAGLHK FDQKKKVSST FNKQCLLTAK S
