位置:首页 > 蛋白库 > MURE_PSEAE
MURE_PSEAE
ID   MURE_PSEAE              Reviewed;         487 AA.
AC   Q59650;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   08-DEC-2000, sequence version 2.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase {ECO:0000255|HAMAP-Rule:MF_00208};
DE            EC=6.3.2.13 {ECO:0000255|HAMAP-Rule:MF_00208};
DE   AltName: Full=Meso-A2pm-adding enzyme {ECO:0000255|HAMAP-Rule:MF_00208};
DE   AltName: Full=Meso-diaminopimelate-adding enzyme {ECO:0000255|HAMAP-Rule:MF_00208};
DE   AltName: Full=UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase {ECO:0000255|HAMAP-Rule:MF_00208};
DE   AltName: Full=UDP-MurNAc-tripeptide synthetase {ECO:0000255|HAMAP-Rule:MF_00208};
DE   AltName: Full=UDP-N-acetylmuramyl-tripeptide synthetase {ECO:0000255|HAMAP-Rule:MF_00208};
GN   Name=murE {ECO:0000255|HAMAP-Rule:MF_00208}; OrderedLocusNames=PA4417;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-325.
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=7486937; DOI=10.1128/aac.39.8.1871;
RA   Liao X., Hancock R.E.W.;
RT   "Cloning and characterization of the Pseudomonas aeruginosa pbpB gene
RT   encoding penicillin-binding protein 3.";
RL   Antimicrob. Agents Chemother. 39:1871-1874(1995).
CC   -!- FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the
CC       nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG)
CC       in the biosynthesis of bacterial cell-wall peptidoglycan.
CC       {ECO:0000255|HAMAP-Rule:MF_00208}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + meso-2,6-diaminoheptanedioate + UDP-N-acetyl-alpha-D-
CC         muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-
CC         acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-
CC         diaminoheptanedioate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791,
CC         ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216;
CC         EC=6.3.2.13; Evidence={ECO:0000255|HAMAP-Rule:MF_00208};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00208};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00208}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00208}.
CC   -!- PTM: Carboxylation is probably crucial for Mg(2+) binding and,
CC       consequently, for the gamma-phosphate positioning of ATP.
CC       {ECO:0000255|HAMAP-Rule:MF_00208}.
CC   -!- SIMILARITY: Belongs to the MurCDEF family. MurE subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00208}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE004091; AAG07805.1; -; Genomic_DNA.
DR   EMBL; X84053; CAA58873.1; -; Genomic_DNA.
DR   PIR; B83095; B83095.
DR   PIR; S54873; S54873.
DR   RefSeq; NP_253107.1; NC_002516.2.
DR   RefSeq; WP_003112751.1; NZ_QZGE01000004.1.
DR   AlphaFoldDB; Q59650; -.
DR   SMR; Q59650; -.
DR   STRING; 287.DR97_1595; -.
DR   PaxDb; Q59650; -.
DR   PRIDE; Q59650; -.
DR   DNASU; 881246; -.
DR   EnsemblBacteria; AAG07805; AAG07805; PA4417.
DR   GeneID; 881246; -.
DR   KEGG; pae:PA4417; -.
DR   PATRIC; fig|208964.12.peg.4626; -.
DR   PseudoCAP; PA4417; -.
DR   HOGENOM; CLU_022291_3_2_6; -.
DR   InParanoid; Q59650; -.
DR   OMA; CFMEVSS; -.
DR   PhylomeDB; Q59650; -.
DR   BioCyc; PAER208964:G1FZ6-4504-MON; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008765; F:UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate 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; 3.40.1190.10; -; 1.
DR   Gene3D; 3.90.190.20; -; 1.
DR   HAMAP; MF_00208; MurE; 1.
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; IPR035911; MurE/MurF_N.
DR   InterPro; IPR005761; UDP-N-AcMur-Glu-dNH2Pim_ligase.
DR   Pfam; PF01225; Mur_ligase; 1.
DR   Pfam; PF02875; Mur_ligase_C; 1.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   SUPFAM; SSF53244; SSF53244; 1.
DR   SUPFAM; SSF53623; SSF53623; 1.
DR   SUPFAM; SSF63418; SSF63418; 1.
DR   TIGRFAMs; TIGR01085; murE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell cycle; Cell division; Cell shape;
KW   Cell wall biogenesis/degradation; Cytoplasm; Ligase; Magnesium;
KW   Nucleotide-binding; Peptidoglycan synthesis; Reference proteome.
FT   CHAIN           1..487
FT                   /note="UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-
FT                   diaminopimelate ligase"
FT                   /id="PRO_0000101926"
FT   MOTIF           402..405
FT                   /note="Meso-diaminopimelate recognition motif"
FT   BINDING         23
FT                   /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT                   glutamate"
FT                   /ligand_id="ChEBI:CHEBI:83900"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT   BINDING         25
FT                   /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT                   glutamate"
FT                   /ligand_id="ChEBI:CHEBI:83900"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT   BINDING         108..114
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT   BINDING         150..151
FT                   /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT                   glutamate"
FT                   /ligand_id="ChEBI:CHEBI:83900"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT   BINDING         177
FT                   /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT                   glutamate"
FT                   /ligand_id="ChEBI:CHEBI:83900"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT   BINDING         183
FT                   /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT                   glutamate"
FT                   /ligand_id="ChEBI:CHEBI:83900"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT   BINDING         185
FT                   /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT                   glutamate"
FT                   /ligand_id="ChEBI:CHEBI:83900"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT   BINDING         378
FT                   /ligand="meso-2,6-diaminoheptanedioate"
FT                   /ligand_id="ChEBI:CHEBI:57791"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT   BINDING         402..405
FT                   /ligand="meso-2,6-diaminoheptanedioate"
FT                   /ligand_id="ChEBI:CHEBI:57791"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT   BINDING         453
FT                   /ligand="meso-2,6-diaminoheptanedioate"
FT                   /ligand_id="ChEBI:CHEBI:57791"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT   BINDING         457
FT                   /ligand="meso-2,6-diaminoheptanedioate"
FT                   /ligand_id="ChEBI:CHEBI:57791"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT   MOD_RES         217
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT   CONFLICT        6
FT                   /note="N -> S (in Ref. 2; CAA58873)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        26
FT                   /note="R -> H (in Ref. 2; CAA58873)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        31
FT                   /note="G -> V (in Ref. 2; CAA58873)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        36
FT                   /note="A -> T (in Ref. 2; CAA58873)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        41
FT                   /note="R -> H (in Ref. 2; CAA58873)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        53
FT                   /note="A -> T (in Ref. 2; CAA58873)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        57
FT                   /note="A -> T (in Ref. 2; CAA58873)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        225
FT                   /note="G -> D (in Ref. 2; CAA58873)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   487 AA;  51263 MW;  2B6DC9740C00BFDD CRC64;
     MPMSLNQLFP QAERDLLIRE LTLDSRGVRP GDLFLAVPGG RQDGRAHIAD ALAKGAAAVA
     YEAEGAGELP PSDAPLIAVK GLAAQLSAVA GRFYGEPSRG LDLIGVTGTN GKTSVSQLVA
     QALDLLGERC GIVGTLGTGF YGALESGRHT TPDPLAVQAT LATLKQAGAR AVAMEVSSHG
     LDQGRVAALG FDIAVFTNLS RDHLDYHGSM EAYAAAKAKL FAWPGLRCRV INLDDDFGRR
     LAGEEQDSEL ITYSLTDSSA FLYCREARFG DAGIEAALVT PHGEGLLRSP LLGRFNLSNL
     LAAVGALLGL GYPLGDILRT LPQLQGPVGR MQRLGGGDKP LVVVDYAHTP DALEKVLEAL
     RPHAAARLLC LFGCGGDRDA GKRPLMAAIA ERLADEVLVT DDNPRTEASA AIIADIRKGF
     AAADKVTFLP SRGEAIAHLI ASAAVDDVVL LAGKGHEDYQ EIDGVRHPFS DIEQAERALA
     AWEVPHA
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024