GenomeNet

Database: UniProt
Entry: Q821S4
LinkDB: Q821S4
Original site: Q821S4 
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   16-JAN-2019, entry version 116.
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   Chlamydophila caviae (strain GPIC).
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=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.,
RA   Carty H.A., Umayam L.A., Haft D.H., Peterson J.D., Beanan M.J.,
RA   White O., Salzberg S.L., Hsia R.-C., McClarty G., Rank R.G.,
RA   Bavoil P.M., 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 +
CC         H(+) + 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.
CC       {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
CC       family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the D-alanine--
CC       D-alanine ligase family. {ECO:0000305}.
DR   EMBL; AE015925; AAP05604.1; -; Genomic_DNA.
DR   RefSeq; WP_011006818.1; NC_003361.3.
DR   ProteinModelPortal; Q821S4; -.
DR   SMR; Q821S4; -.
DR   STRING; 227941.CCA00863; -.
DR   PRIDE; Q821S4; -.
DR   EnsemblBacteria; AAP05604; AAP05604; CCA_00863.
DR   KEGG; cca:CCA_00863; -.
DR   eggNOG; ENOG4105DFU; Bacteria.
DR   eggNOG; COG0773; LUCA.
DR   eggNOG; COG1181; LUCA.
DR   KO; K01921; -.
DR   KO; K01924; -.
DR   OMA; INRQGLW; -.
DR   OrthoDB; 307881at2; -.
DR   BioCyc; CCAV227941:G1G03-871-MONOMER; -.
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; Complete proteome; Cytoplasm;
KW   Ligase; Magnesium; Manganese; Metal-binding; Multifunctional enzyme;
KW   Nucleotide-binding; Peptidoglycan synthesis.
FT   CHAIN         1    811       Bifunctional enzyme MurC/Ddl.
FT                                /FTId=PRO_0000177913.
FT   DOMAIN      574    785       ATP-grasp.
FT   NP_BIND     111    117       ATP. {ECO:0000255}.
FT   NP_BIND     607    662       ATP. {ECO:0000250}.
FT   REGION        1    450       UDP-N-acetylmuramate--alanine ligase.
FT   REGION      451    811       D-alanine--D-alanine ligase.
FT   METAL       739    739       Magnesium or manganese 1. {ECO:0000250}.
FT   METAL       752    752       Magnesium or manganese 1. {ECO:0000250}.
FT   METAL       752    752       Magnesium or manganese 2. {ECO:0000250}.
FT   METAL       754    754       Magnesium or manganese 2. {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
//
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