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MUDD_CHLPN
ID   MUDD_CHLPN              Reviewed;         809 AA.
AC   Q9Z701; Q9JQB5;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 166.
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=CPn_0905, CP_0961, CpB0937;
OS   Chlamydia pneumoniae (Chlamydophila pneumoniae).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=83558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CWL029;
RX   PubMed=10192388; DOI=10.1038/7716;
RA   Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W.,
RA   Olinger L., Grimwood J., Davis R.W., Stephens R.S.;
RT   "Comparative genomes of Chlamydia pneumoniae and C. trachomatis.";
RL   Nat. Genet. 21:385-389(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AR39;
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).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J138;
RX   PubMed=10871362; DOI=10.1093/nar/28.12.2311;
RA   Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K.,
RA   Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.;
RT   "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from
RT   Japan and CWL029 from USA.";
RL   Nucleic Acids Res. 28:2311-2314(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TW-183;
RA   Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P.,
RA   Schneider S., Pohl T., Essig A., Marre R., Melchers K.;
RT   "The genome sequence of Chlamydia pneumoniae TW183 and comparison with
RT   other Chlamydia strains based on whole genome sequence analysis.";
RL   Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
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; AE001363; AAD19043.1; -; Genomic_DNA.
DR   EMBL; AE002161; AAF38741.1; -; Genomic_DNA.
DR   EMBL; BA000008; BAA99113.1; -; Genomic_DNA.
DR   EMBL; AE009440; AAP98866.1; -; Genomic_DNA.
DR   PIR; D72022; D72022.
DR   PIR; G86603; G86603.
DR   RefSeq; NP_225100.1; NC_000922.1.
DR   RefSeq; WP_010883540.1; NZ_LN847257.1.
DR   AlphaFoldDB; Q9Z701; -.
DR   SMR; Q9Z701; -.
DR   STRING; 115711.CP_0961; -.
DR   EnsemblBacteria; AAD19043; AAD19043; CPn_0905.
DR   EnsemblBacteria; AAF38741; AAF38741; CP_0961.
DR   KEGG; cpa:CP_0961; -.
DR   KEGG; cpj:murC_ddlA; -.
DR   KEGG; cpn:CPn_0905; -.
DR   KEGG; cpt:CpB0937; -.
DR   PATRIC; fig|115713.3.peg.986; -.
DR   eggNOG; COG0773; Bacteria.
DR   eggNOG; COG1181; Bacteria.
DR   HOGENOM; CLU_019395_0_0_0; -.
DR   OrthoDB; 764798at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000583; Chromosome.
DR   Proteomes; UP000000801; 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..809
FT                   /note="Bifunctional enzyme MurC/Ddl"
FT                   /id="PRO_0000177915"
FT   DOMAIN          573..784
FT                   /note="ATP-grasp"
FT   REGION          1..450
FT                   /note="UDP-N-acetylmuramate--alanine ligase"
FT   REGION          451..809
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         606..661
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         738
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         751
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         751
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         753
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        560
FT                   /note="L -> P (in Ref. 4; AAP98866)"
FT                   /evidence="ECO:0000305"
SQ   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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