(data stored in SCRATCH zone)

SWISSPROT: B7UID8_ECO27

ID   B7UID8_ECO27            Unreviewed;       438 AA.
AC   B7UID8;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 68.
DE   RecName: Full=UDP-N-acetylmuramoylalanine--D-glutamate ligase {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01178103};
DE            EC=6.3.2.9 {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01178084};
DE   AltName: Full=D-glutamic acid-adding enzyme {ECO:0000256|HAMAP-Rule:MF_00639};
DE   AltName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase {ECO:0000256|HAMAP-Rule:MF_00639};
GN   Name=murD {ECO:0000256|HAMAP-Rule:MF_00639,
GN   ECO:0000313|EMBL:CAS07641.1};
GN   OrderedLocusNames=E2348C_0093 {ECO:0000313|EMBL:CAS07641.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS07641.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS07641.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
CC   -!- FUNCTION: Cell wall formation. Catalyzes the addition of glutamate
CC       to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
CC       {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664,
CC       ECO:0000256|SAAS:SAAS01178092}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-
CC         alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-
CC         muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900,
CC         ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00639, ECO:0000256|RuleBase:RU003664,
CC         ECO:0000256|SAAS:SAAS01178088};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664,
CC       ECO:0000256|SAAS:SAAS00084431}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00639,
CC       ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382026}.
CC   -!- SIMILARITY: Belongs to the MurCDEF family. {ECO:0000256|HAMAP-
CC       Rule:MF_00639, ECO:0000256|SAAS:SAAS00569906}.
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DR   EMBL; FM180568; CAS07641.1; -; Genomic_DNA.
DR   RefSeq; WP_000796458.1; NC_011601.1.
DR   EnsemblBacteria; CAS07641; CAS07641; E2348C_0093.
DR   KEGG; ecg:E2348C_0093; -.
DR   HOGENOM; HOG000049427; -.
DR   KO; K01925; -.
DR   OMA; VDKGNDY; -.
DR   BioCyc; ECOL574521:E2348C_RS00480-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000008205; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008764; F:UDP-N-acetylmuramoylalanine-D-glutamate 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_00639; MurD; 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; IPR005762; UDP-N-AcMur-Glu_ligase.
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; TIGR01087; murD; 1.
PE   3: Inferred from homology;
DR   PRODOM; B7UID8.
DR   SWISS-2DPAGE; B7UID8.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00639,
KW   ECO:0000256|SAAS:SAAS00459147};
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_00639,
KW   ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00084569};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_00639,
KW   ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00459144};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_00639,
KW   ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00459184};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00639,
KW   ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00084482};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00639,
KW   ECO:0000256|SAAS:SAAS00459072};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00639,
KW   ECO:0000256|SAAS:SAAS00459180, ECO:0000313|EMBL:CAS07641.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00639,
KW   ECO:0000256|SAAS:SAAS00084387};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00639,
KW   ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00459171}.
FT   DOMAIN      110    280       Mur_ligase_M. {ECO:0000259|Pfam:PF08245}.
FT   DOMAIN      301    373       Mur_ligase_C. {ECO:0000259|Pfam:PF02875}.
FT   NP_BIND     112    118       ATP. {ECO:0000256|HAMAP-Rule:MF_00639}.
SQ   SEQUENCE   438 AA;  46881 MW;  E3054A694AEABE04 CRC64;
     MADYQGKNVV IIGLGLTGLS CVDFFLARGV TPRVMDTRMT PPGLDKLPEA VERHTGGLND
     EWLMAADLIV ASPGIALAHP SLSAAADAGI EIVGDIELFC REAQAPIVAI TGSNGKSTVT
     TLVGEMAKAA GVNVGVGGNI GLPALMLLDD ECELYVLELS SFQLETTSSL QAVAATILNV
     TEDHMDRYPF GLQQYRAAKL RIYENAKVCV VNADDALTMP IRGADERCVS FGVNMGDYHL
     NHQQGETWLR VKGEKVLNVK EMKLSGQHNY TNALAALALA DAAGLPRASS LKALTTFTGL
     PHRFEVVLEH NGVCWVNDSK ATNVGSTEAA LNGLHVDGTL HLLLGGDGKS ADFSPLARYL
     NGDNVRLYCF GRDGAQLAAL RPEVAEQTET MEQAMRLLAT RVQPGDMVLL SPACASLDQF
     KNFEQRGNEF ARLAKELG
//

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