位置:首页 > 蛋白库 > MURC_ZYMMO
MURC_ZYMMO
ID   MURC_ZYMMO              Reviewed;         476 AA.
AC   Q9RNM7; Q5NPA4;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 2.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=UDP-N-acetylmuramate--L-alanine ligase {ECO:0000255|HAMAP-Rule:MF_00046};
DE            EC=6.3.2.8 {ECO:0000255|HAMAP-Rule:MF_00046};
DE   AltName: Full=UDP-N-acetylmuramoyl-L-alanine synthetase {ECO:0000255|HAMAP-Rule:MF_00046};
GN   Name=murC {ECO:0000255|HAMAP-Rule:MF_00046}; OrderedLocusNames=ZMO0832;
OS   Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Zymomonadaceae; Zymomonas.
OX   NCBI_TaxID=264203;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 31821 / ZM4 / CP4;
RA   Um H.W., Kang H.S.;
RL   Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31821 / ZM4 / CP4;
RX   PubMed=15592456; DOI=10.1038/nbt1045;
RA   Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA   Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA   Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA   Kang H.S.;
RT   "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT   ZM4.";
RL   Nat. Biotechnol. 23:63-68(2005).
CC   -!- FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00046}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00046};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00046}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00046}.
CC   -!- SIMILARITY: Belongs to the MurCDEF family. {ECO:0000255|HAMAP-
CC       Rule:MF_00046}.
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; AF179611; AAD53935.1; -; Genomic_DNA.
DR   EMBL; AE008692; AAV89456.1; -; Genomic_DNA.
DR   RefSeq; WP_011240702.1; NZ_CP035711.1.
DR   AlphaFoldDB; Q9RNM7; -.
DR   SMR; Q9RNM7; -.
DR   STRING; 264203.ZMO0832; -.
DR   EnsemblBacteria; AAV89456; AAV89456; ZMO0832.
DR   GeneID; 58026640; -.
DR   KEGG; zmo:ZMO0832; -.
DR   eggNOG; COG0773; Bacteria.
DR   HOGENOM; CLU_028104_2_2_5; -.
DR   OMA; DITYQLR; -.
DR   OrthoDB; 307881at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001173; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; 3.40.1190.10; -; 1.
DR   Gene3D; 3.90.190.20; -; 1.
DR   HAMAP; MF_00046; MurC; 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; IPR005758; UDP-N-AcMur_Ala_ligase_MurC.
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   TIGRFAMs; TIGR01082; murC; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell cycle; Cell division; Cell shape;
KW   Cell wall biogenesis/degradation; Cytoplasm; Ligase; Nucleotide-binding;
KW   Peptidoglycan synthesis; Reference proteome.
FT   CHAIN           1..476
FT                   /note="UDP-N-acetylmuramate--L-alanine ligase"
FT                   /id="PRO_0000182192"
FT   BINDING         115..121
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00046"
FT   CONFLICT        331
FT                   /note="G -> C (in Ref. 1; AAD53935)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        373
FT                   /note="S -> L (in Ref. 1; AAD53935)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        451
FT                   /note="L -> V (in Ref. 1; AAD53935)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        462..476
FT                   /note="GLAADITSIREVHHL -> VLRQILPQSERFITYDDCYIFQYLK (in
FT                   Ref. 1; AAD53935)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   476 AA;  51023 MW;  29112C60EF8F69B0 CRC64;
     MKGVGTDIGR IHFVGIGGIG MSGIAEVMHN LGYQVQGSDI SEGYTVDALR QMGIKVLIGH
     HAENVKDAAV VVVSSAIHRG NPEVEAALEN RIPVVRRAEM LAELMRLKST VAVAGTHGKT
     TTTSMVAALL DAGGIDPTVI NGGIINSYGS NARLGDSDWM VVEADESDGS FLRLDGTLAI
     VTNIDPEHLD HYGSFEKVQD AFVEFVSNVP FYGAAFLCID HPVVQSILPR IRDRRLITYG
     FSAQADIRAV DITPISGGNR FTAVIRGRDG DIRRIENIFL PMPGRHNIQN ALSAIGVALE
     FSIPDAAIRD GFARFGGVKR RFSRVGEIKI GDGSVLVIDD YGHHPVEIKA VLSAARESAQ
     QRVIAVVQPH RFSRLHDLMT EFQSAFNDAD MVFVAPVYAA GEQPIAGVDS QALVSGLKQH
     GHRSAQAVDS PRSLAIALAD IIKADDIIIC LGAGDITKWA AGLAADITSI REVHHL
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024