(data stored in SCRATCH zone)

SWISSPROT: C8U1F8_ECO10

ID   C8U1F8_ECO10            Unreviewed;       452 AA.
AC   C8U1F8;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 69.
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:BAI28966.1};
GN   OrderedLocusNames=ECO103_0088 {ECO:0000313|EMBL:BAI28966.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI28966.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI28966.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(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; AP010958; BAI28966.1; -; Genomic_DNA.
DR   RefSeq; WP_000626688.1; NC_013353.1.
DR   SMR; C8U1F8; -.
DR   EnsemblBacteria; BAI28966; BAI28966; ECO103_0088.
DR   KEGG; eoh:ECO103_0088; -.
DR   HOGENOM; HOG000268120; -.
DR   KO; K01929; -.
DR   OMA; SYNNHWG; -.
DR   BioCyc; ECOL585395:ECO103_RS00445-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000959; 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; C8U1F8.
DR   SWISS-2DPAGE; C8U1F8.
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:UP000000959};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02019};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_02019, ECO:0000313|EMBL:BAI28966.1};
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;  47421 MW;  B47D966C2DBBC572 CRC64;
     MISVTLSQLT DILNGELQGA DITLDAVTTD TRKLTPGCLF VALKGERFDA HDFADQAKAG
     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 QLAENQLLLD DSYNANVGSM TAAVQVLAEM PGYRVLVVGD
     MAELGAESEA CHVQVGEAAK AAGIDRVLSV GKQSHAISTA SGVGEHFADK TALITRLKSL
     IAEQQVITIL VKGSRSAAME EVVRALQENG TC
//

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