(data stored in ACNUC10821 zone)

SWISSPROT: C8U1G3_ECO10

ID   C8U1G3_ECO10            Unreviewed;       491 AA.
AC   C8U1G3;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 66.
DE   RecName: Full=UDP-N-acetylmuramate--L-alanine ligase {ECO:0000256|HAMAP-Rule:MF_00046, ECO:0000256|SAAS:SAAS01090471};
DE            EC=6.3.2.8 {ECO:0000256|HAMAP-Rule:MF_00046, ECO:0000256|SAAS:SAAS01090477};
DE   AltName: Full=UDP-N-acetylmuramoyl-L-alanine synthetase {ECO:0000256|HAMAP-Rule:MF_00046};
GN   Name=murC {ECO:0000256|HAMAP-Rule:MF_00046,
GN   ECO:0000313|EMBL:BAI28971.1};
GN   OrderedLocusNames=ECO103_0093 {ECO:0000313|EMBL:BAI28971.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI28971.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI28971.1, 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: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00046,
CC       ECO:0000256|SAAS:SAAS01090476}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP +
CC         H(+) + 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:0000256|HAMAP-Rule:MF_00046,
CC         ECO:0000256|SAAS:SAAS01124320};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00046, ECO:0000256|SAAS:SAAS00085119}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00046,
CC       ECO:0000256|SAAS:SAAS00085149}.
CC   -!- SIMILARITY: Belongs to the MurCDEF family. {ECO:0000256|HAMAP-
CC       Rule:MF_00046, ECO:0000256|SAAS:SAAS01090475}.
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DR   EMBL; AP010958; BAI28971.1; -; Genomic_DNA.
DR   RefSeq; WP_001096048.1; NC_013353.1.
DR   SMR; C8U1G3; -.
DR   EnsemblBacteria; BAI28971; BAI28971; ECO103_0093.
DR   KEGG; eoh:ECO103_0093; -.
DR   HOGENOM; HOG000256031; -.
DR   KO; K01924; -.
DR   OMA; LTMGAGD; -.
DR   BioCyc; ECOL585395:ECO103_RS00470-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: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;
DR   PRODOM; C8U1G3.
DR   SWISS-2DPAGE; C8U1G3.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00046,
KW   ECO:0000256|SAAS:SAAS00459234};
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_00046,
KW   ECO:0000256|SAAS:SAAS00459266};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_00046,
KW   ECO:0000256|SAAS:SAAS00459376};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_00046,
KW   ECO:0000256|SAAS:SAAS00459316};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00046,
KW   ECO:0000256|SAAS:SAAS00459280};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00046,
KW   ECO:0000256|SAAS:SAAS00459252};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00046,
KW   ECO:0000256|SAAS:SAAS00459220, ECO:0000313|EMBL:BAI28971.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00046,
KW   ECO:0000256|SAAS:SAAS00459312};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00046,
KW   ECO:0000256|SAAS:SAAS00459348}.
FT   DOMAIN       21    118       Mur_ligase. {ECO:0000259|Pfam:PF01225}.
FT   DOMAIN      124    304       Mur_ligase_M. {ECO:0000259|Pfam:PF08245}.
FT   DOMAIN      327    418       Mur_ligase_C. {ECO:0000259|Pfam:PF02875}.
FT   NP_BIND     126    132       ATP. {ECO:0000256|HAMAP-Rule:MF_00046}.
SQ   SEQUENCE   491 AA;  53598 MW;  6FB5235931C01008 CRC64;
     MNTQQLAKLR SIVPEMRRVR HIHFVGIGGA GMGGIAEVLA NEGYQISGSD LAPNPVTQQL
     MNLGATIYFN HRPENVRDAS VVVVSSAISA DNPEIVAAHE ARIPVIRRAE MLAELMRFRH
     GIAIAGTHGK TTTTAMVSSI YAEAGLDPTF VNGGLVKAAG VHARLGHGRY LIAEADESDA
     SFLHLQPMVA IVTNIEADHM DTYQGDFENL KQTFINFLHN LPFYGRAVMC VDDPVIRELL
     PRVGRQTTTY GFSEDADVRV EDYQQIGPQG HFTLLRQDKE PMRVTLNAPG RHNALNAAAA
     VAVATEEGID DEAILRALES FQGTGRRFDF LGEFPLEPVN GKSGTAMLVD DYGHHPTEVD
     ATIKAARAGW PDKNLVMLFQ PHRFTRTRDL YDDFANVLTQ VDTLLMLEVY PAGEAPIPGA
     DSRSLCRTIR GRGKIDPILV PDPAQVAEML APVLTGNDLI LVQGAGNIGK IARSLAEIKL
     KPQTPEEEQH D
//

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