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Bifunctional enzyme MurC/Ddl [Includes: UDP-N-acetylmuramate--L-alanine ligase (EC 6.3.2.8) (UDP-N-acetylmuramoyl-L-alanine synthetase); D-alanine--D-alanine ligase (EC 6.3.2.4) (D-Ala-D-Ala ligase) (D-alanylalanine synthetase)]

 MUDD_CHLPN              Reviewed;         809 AA.
Q9Z701; Q9JQB5;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
22-NOV-2017, entry version 147.
RecName: Full=Bifunctional enzyme MurC/Ddl;
Includes:
RecName: Full=UDP-N-acetylmuramate--L-alanine ligase;
EC=6.3.2.8;
AltName: Full=UDP-N-acetylmuramoyl-L-alanine synthetase;
Includes:
RecName: Full=D-alanine--D-alanine ligase;
EC=6.3.2.4;
AltName: Full=D-Ala-D-Ala ligase;
AltName: Full=D-alanylalanine synthetase;
Name=murC/ddl; OrderedLocusNames=CPn_0905, CP_0961, CpB0937;
Chlamydia pneumoniae (Chlamydophila pneumoniae).
Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
Chlamydia/Chlamydophila group; Chlamydia.
NCBI_TaxID=83558;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CWL029;
PubMed=10192388; DOI=10.1038/7716;
Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W.,
Olinger L., Grimwood J., Davis R.W., Stephens R.S.;
"Comparative genomes of Chlamydia pneumoniae and C. trachomatis.";
Nat. Genet. 21:385-389(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AR39;
PubMed=10684935; DOI=10.1093/nar/28.6.1397;
Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F.,
White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J.,
Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C.,
Dodson R.J., Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F.,
McClarty G., Salzberg S.L., Eisen J.A., Fraser C.M.;
"Genome sequences of Chlamydia trachomatis MoPn and Chlamydia
pneumoniae AR39.";
Nucleic Acids Res. 28:1397-1406(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=J138;
PubMed=10871362; DOI=10.1093/nar/28.12.2311;
Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K.,
Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.;
"Comparison of whole genome sequences of Chlamydia pneumoniae J138
from Japan and CWL029 from USA.";
Nucleic Acids Res. 28:2311-2314(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=TW-183;
Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P.,
Schneider S., Pohl T., Essig A., Marre R., Melchers K.;
"The genome sequence of Chlamydia pneumoniae TW183 and comparison with
other Chlamydia strains based on whole genome sequence analysis.";
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Cell wall formation. {ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + UDP-N-acetyl-alpha-D-muramate + L-
alanine = ADP + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-
alanine.
-!- CATALYTIC ACTIVITY: ATP + 2 D-alanine = ADP + phosphate + D-
alanyl-D-alanine.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
Note=Binds 2 magnesium or manganese ions per subunit.
{ECO:0000250};
-!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- SIMILARITY: In the N-terminal section; belongs to the MurCDEF
family. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the D-alanine--
D-alanine ligase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AE001363; AAD19043.1; -; Genomic_DNA.
EMBL; AE002161; AAF38741.1; -; Genomic_DNA.
EMBL; BA000008; BAA99113.1; -; Genomic_DNA.
EMBL; AE009440; AAP98866.1; -; Genomic_DNA.
PIR; D72022; D72022.
PIR; G86603; G86603.
RefSeq; NP_225100.1; NC_000922.1.
RefSeq; WP_010883540.1; NZ_LN847257.1.
ProteinModelPortal; Q9Z701; -.
SMR; Q9Z701; -.
STRING; 182082.CpB0937; -.
EnsemblBacteria; AAD19043; AAD19043; CPn_0905.
EnsemblBacteria; AAF38741; AAF38741; CP_0961.
EnsemblBacteria; AAP98866; AAP98866; CpB0937.
EnsemblBacteria; BAA99113; BAA99113; BAA99113.
GeneID; 895305; -.
KEGG; cpa:CP_0961; -.
KEGG; cpj:murC_ddlA; -.
KEGG; cpn:CPn0905; -.
KEGG; cpt:CpB0937; -.
PATRIC; fig|115713.3.peg.986; -.
eggNOG; ENOG4105DFU; Bacteria.
eggNOG; COG0773; LUCA.
eggNOG; COG1181; LUCA.
HOGENOM; HOG000034913; -.
KO; K01921; -.
KO; K01924; -.
OrthoDB; POG091H02MF; -.
UniPathway; UPA00219; -.
Proteomes; UP000000583; Chromosome.
Proteomes; UP000000801; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008763; F:UDP-N-acetylmuramate-L-alanine ligase activity; IEA:UniProtKB-EC.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
Gene3D; 3.30.1490.20; -; 1.
Gene3D; 3.40.1190.10; -; 1.
Gene3D; 3.90.190.20; -; 1.
HAMAP; MF_00047; Dala_Dala_lig; 1.
HAMAP; MF_00046; MurC; 1.
InterPro; IPR011761; ATP-grasp.
InterPro; IPR013815; ATP_grasp_subdomain_1.
InterPro; IPR000291; D-Ala_lig_Van_CS.
InterPro; IPR005905; D_ala_D_ala.
InterPro; IPR011095; Dala_Dala_lig_C.
InterPro; IPR011127; Dala_Dala_lig_N.
InterPro; IPR036565; Mur-like_cat_sf.
InterPro; IPR004101; Mur_ligase_C.
InterPro; IPR036615; Mur_ligase_C_dom_sf.
InterPro; IPR013221; Mur_ligase_cen.
InterPro; IPR000713; Mur_ligase_N.
InterPro; IPR016185; PreATP-grasp_dom_sf.
InterPro; IPR005758; UDP-N-AcMur_Ala_ligase_murC.
Pfam; PF07478; Dala_Dala_lig_C; 1.
Pfam; PF01820; Dala_Dala_lig_N; 1.
Pfam; PF01225; Mur_ligase; 1.
Pfam; PF02875; Mur_ligase_C; 1.
Pfam; PF08245; Mur_ligase_M; 1.
SUPFAM; SSF52440; SSF52440; 1.
SUPFAM; SSF53244; SSF53244; 1.
SUPFAM; SSF53623; SSF53623; 1.
TIGRFAMs; TIGR01205; D_ala_D_alaTIGR; 1.
TIGRFAMs; TIGR01082; murC; 1.
PROSITE; PS50975; ATP_GRASP; 1.
PROSITE; PS00843; DALA_DALA_LIGASE_1; 1.
PROSITE; PS00844; DALA_DALA_LIGASE_2; 1.
3: Inferred from homology;
ATP-binding; Cell cycle; Cell division; Cell shape;
Cell wall biogenesis/degradation; Complete proteome; Cytoplasm;
Ligase; Magnesium; Manganese; Metal-binding; Multifunctional enzyme;
Nucleotide-binding; Peptidoglycan synthesis; Reference proteome.
CHAIN 1 809 Bifunctional enzyme MurC/Ddl.
/FTId=PRO_0000177915.
DOMAIN 573 784 ATP-grasp.
NP_BIND 111 117 ATP. {ECO:0000255}.
NP_BIND 606 661 ATP. {ECO:0000250}.
REGION 1 450 UDP-N-acetylmuramate--alanine ligase.
REGION 451 809 D-alanine--D-alanine ligase.
METAL 738 738 Magnesium or manganese 1. {ECO:0000250}.
METAL 751 751 Magnesium or manganese 1. {ECO:0000250}.
METAL 751 751 Magnesium or manganese 2. {ECO:0000250}.
METAL 753 753 Magnesium or manganese 2. {ECO:0000250}.
CONFLICT 560 560 L -> P (in Ref. 4; AAP98866).
{ECO:0000305}.
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


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