(data stored in ACNUC7421 zone)

SWISSPROT: B7UID6_ECO27

ID   B7UID6_ECO27            Unreviewed;       452 AA.
AC   B7UID6;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   16-JAN-2019, entry version 67.
DE   RecName: Full=UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase {ECO:0000256|HAMAP-Rule:MF_02019, ECO:0000256|RuleBase:RU004136};
DE            EC=6.3.2.10 {ECO:0000256|HAMAP-Rule:MF_02019, ECO:0000256|RuleBase:RU004136};
DE   AltName: Full=D-alanyl-D-alanine-adding enzyme {ECO:0000256|HAMAP-Rule:MF_02019};
GN   Name=murF {ECO:0000256|HAMAP-Rule:MF_02019,
GN   ECO:0000313|EMBL:CAS07639.1};
GN   OrderedLocusNames=E2348C_0091 {ECO:0000313|EMBL:CAS07639.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS07639.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS07639.1, 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: Involved in cell wall formation. Catalyzes the final
CC       step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the
CC       precursor of murein. {ECO:0000256|HAMAP-Rule:MF_02019,
CC       ECO:0000256|RuleBase:RU004136}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-muramoyl-
CC         L-alanyl-gamma-D-glutamyl-L-lysine = ADP + H(+) + phosphate +
CC         UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-
CC         D-alanyl-D-alanine; Xref=Rhea:RHEA:16085, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57822,
CC         ChEBI:CHEBI:70758, ChEBI:CHEBI:83903, ChEBI:CHEBI:456216;
CC         EC=6.3.2.10; Evidence={ECO:0000256|HAMAP-Rule:MF_02019,
CC         ECO:0000256|RuleBase:RU004136};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_02019, ECO:0000256|RuleBase:RU004136}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02019,
CC       ECO:0000256|RuleBase:RU004136}.
CC   -!- SIMILARITY: Belongs to the MurCDEF family. MurF subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_02019}.
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DR   EMBL; FM180568; CAS07639.1; -; Genomic_DNA.
DR   RefSeq; WP_000626710.1; NC_011601.1.
DR   EnsemblBacteria; CAS07639; CAS07639; E2348C_0091.
DR   KEGG; ecg:E2348C_0091; -.
DR   HOGENOM; HOG000268120; -.
DR   KO; K01929; -.
DR   OMA; SYNNHWG; -.
DR   BioCyc; ECOL574521:E2348C_RS00470-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:0047480; F:UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-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_02019; MurF; 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; IPR005863; UDP-N-AcMur_synth.
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; TIGR01143; murF; 1.
PE   3: Inferred from homology;
DR   PRODOM; B7UID6.
DR   SWISS-2DPAGE; B7UID6.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_02019};
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_02019,
KW   ECO:0000256|RuleBase:RU004136};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_02019,
KW   ECO:0000256|RuleBase:RU004136};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_02019,
KW   ECO:0000256|RuleBase:RU004136};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_02019,
KW   ECO:0000256|RuleBase:RU004136};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02019};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_02019, ECO:0000313|EMBL:CAS07639.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02019};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_02019,
KW   ECO:0000256|RuleBase:RU004136}.
FT   DOMAIN       26     80       Mur_ligase. {ECO:0000259|Pfam:PF01225}.
FT   DOMAIN      106    292       Mur_ligase_M. {ECO:0000259|Pfam:PF08245}.
FT   DOMAIN      313    394       Mur_ligase_C. {ECO:0000259|Pfam:PF02875}.
FT   NP_BIND     107    113       ATP. {ECO:0000256|HAMAP-Rule:MF_02019}.
SQ   SEQUENCE   452 AA;  47296 MW;  B7C2EE7185035DEE CRC64;
     MISVTLSQLT DILNGELQGA DITLDAVTTD TRKLTPGCLF VALKGERFDA HDFAGQAKAG
     GAGALLVSRP LDIDLPQLIV KDTRLAFGEL AAWVRQQVPA RVVALTGSSG KTSVKEMTAA
     ILSQCGNTLY TAGNLNNDIG VPMTLLRLTP EYDYAVIELG ANHQGEIAWT VSLTRPEAAL
     VNNLAAAHLE GFGSLAGVAK AKGEIFSGLP ENGIAIMNAD NNDWLNWQSV IGSRKVWRFS
     PNAANSDFTA TNIHVTSHGT EFTLQTPTGS VDVLLPLPGR HNIANALAAA ALSMSVGATL
     DAIKAGLANL KAVPGRLFPI KLAENQLLLD DSYNANVGSM TAAVQVLAEM PGYRVLVVGD
     MAELGAESEA CHVQVGEAAK AAGIDCVLSV GKQSHAISTA SGVGEHFSDK TALIARLKSL
     IAEQQVITIL VKGSRSAAME EVVRALQENG TC
//

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