(data stored in ACNUC7421 zone)

SWISSPROT: B7UID5_ECO27

ID   B7UID5_ECO27            Unreviewed;       495 AA.
AC   B7UID5;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   16-JAN-2019, entry version 70.
DE   RecName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase {ECO:0000256|HAMAP-Rule:MF_00208};
DE            EC=6.3.2.13 {ECO:0000256|HAMAP-Rule:MF_00208};
DE   AltName: Full=Meso-A2pm-adding enzyme {ECO:0000256|HAMAP-Rule:MF_00208};
DE   AltName: Full=Meso-diaminopimelate-adding enzyme {ECO:0000256|HAMAP-Rule:MF_00208};
DE   AltName: Full=UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase {ECO:0000256|HAMAP-Rule:MF_00208};
DE   AltName: Full=UDP-MurNAc-tripeptide synthetase {ECO:0000256|HAMAP-Rule:MF_00208};
DE   AltName: Full=UDP-N-acetylmuramyl-tripeptide synthetase {ECO:0000256|HAMAP-Rule:MF_00208};
GN   Name=murE {ECO:0000256|HAMAP-Rule:MF_00208,
GN   ECO:0000313|EMBL:CAS07638.1};
GN   OrderedLocusNames=E2348C_0090 {ECO:0000313|EMBL:CAS07638.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS07638.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS07638.1, 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: Catalyzes the addition of meso-diaminopimelic acid to
CC       the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate
CC       (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan.
CC       {ECO:0000256|HAMAP-Rule:MF_00208}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + meso-2,6-diaminopimelate + 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-
CC         diaminopimelate; 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:0000256|HAMAP-Rule:MF_00208};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00208};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00208, ECO:0000256|RuleBase:RU004135,
CC       ECO:0000256|SAAS:SAAS00951514}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00208,
CC       ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951526}.
CC   -!- PTM: Carbamoylation is probably crucial for Mg(2+) binding and,
CC       consequently, for the gamma-phosphate positioning of ATP.
CC       {ECO:0000256|HAMAP-Rule:MF_00208}.
CC   -!- SIMILARITY: Belongs to the MurCDEF family. MurE subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00208, ECO:0000256|SAAS:SAAS00569976}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00208}.
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DR   EMBL; FM180568; CAS07638.1; -; Genomic_DNA.
DR   RefSeq; WP_000775110.1; NC_011601.1.
DR   EnsemblBacteria; CAS07638; CAS07638; E2348C_0090.
DR   KEGG; ecg:E2348C_0090; -.
DR   HOGENOM; HOG000268118; -.
DR   KO; K01928; -.
DR   OMA; CFMEVSS; -.
DR   BioCyc; ECOL574521:E2348C_RS00465-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: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;
DR   PRODOM; B7UID5.
DR   SWISS-2DPAGE; B7UID5.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00208,
KW   ECO:0000256|SAAS:SAAS00951530};
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_00208,
KW   ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951553};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_00208,
KW   ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951537};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_00208,
KW   ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951545};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00208,
KW   ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951523};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00208,
KW   ECO:0000256|SAAS:SAAS00951519};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00208,
KW   ECO:0000256|SAAS:SAAS00951534, ECO:0000313|EMBL:CAS07638.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00208};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00208,
KW   ECO:0000256|SAAS:SAAS00951542};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00208,
KW   ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951548}.
FT   DOMAIN       25    102       Mur_ligase. {ECO:0000259|Pfam:PF01225}.
FT   DOMAIN      114    318       Mur_ligase_M. {ECO:0000259|Pfam:PF08245}.
FT   DOMAIN      339    425       Mur_ligase_C. {ECO:0000259|Pfam:PF02875}.
FT   NP_BIND     116    122       ATP. {ECO:0000256|HAMAP-Rule:MF_00208}.
FT   REGION       44     46       UDP-MurNAc-L-Ala-D-Glu binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00208}.
FT   REGION      158    159       UDP-MurNAc-L-Ala-D-Glu binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00208}.
FT   REGION      414    417       Meso-diaminopimelate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00208}.
FT   MOTIF       414    417       Meso-diaminopimelate recognition motif.
FT                                {ECO:0000256|HAMAP-Rule:MF_00208}.
FT   BINDING      27     27       UDP-MurNAc-L-Ala-D-Glu; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00208}.
FT   BINDING      29     29       UDP-MurNAc-L-Ala-D-Glu.
FT                                {ECO:0000256|HAMAP-Rule:MF_00208}.
FT   BINDING     157    157       UDP-MurNAc-L-Ala-D-Glu.
FT                                {ECO:0000256|HAMAP-Rule:MF_00208}.
FT   BINDING     185    185       UDP-MurNAc-L-Ala-D-Glu.
FT                                {ECO:0000256|HAMAP-Rule:MF_00208}.
FT   BINDING     191    191       UDP-MurNAc-L-Ala-D-Glu.
FT                                {ECO:0000256|HAMAP-Rule:MF_00208}.
FT   BINDING     193    193       UDP-MurNAc-L-Ala-D-Glu.
FT                                {ECO:0000256|HAMAP-Rule:MF_00208}.
FT   BINDING     390    390       Meso-diaminopimelate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00208}.
FT   BINDING     465    465       Meso-diaminopimelate; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00208}.
FT   BINDING     469    469       Meso-diaminopimelate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00208}.
FT   MOD_RES     225    225       N6-carboxylysine. {ECO:0000256|HAMAP-
FT                                Rule:MF_00208}.
SQ   SEQUENCE   495 AA;  53314 MW;  6B281063EB4AB49C CRC64;
     MADRNLRDLL APWVPDAPSR ALREMTLDSR VAAAGDLFVA VVGHQADGRR YIPQAIAQGV
     AAIIAEAKDE ATDGEIREMH GVPVIYLSQL NERLSALAGR FYHEPSDNLR LVGVTGTNGK
     TTTTQLLAQW SQLLGETSAV MGTVGNGLLG KVIPTENTTG SAVDVQHELA GLVDQGATFC
     AMEVSSHGLV QHRVAALKFA ASVFTNLSRD HLDYHGDMEH YEAAKWLLYS EHHCGQAIIN
     ADDEVGRRWL AKLPDAVAVS MEDHINPNCH GRWLKAIDVN YHDSGATIRF SSSWGDGEIE
     SHLMGAFNVS NLLLALATLL ALGYPLADLL KTAARLQPVC GRMEVFTAPG KPTVVVDYAH
     TPDALEKALQ AARLHCAGKL WCVFGCGGDR DKGKRPLMGA IAEEFADVAV VTDDNPRTEE
     PRAIINDILA GMLDAGYAKV MEGRAEAVTC AVMQAKENDV VLVAGKGHED YQIVGNQRLD
     YSDRVTVARL LGGIA
//

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