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MURC_SHIB3
ID   MURC_SHIB3              Reviewed;         491 AA.
AC   B2U296;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=UDP-N-acetylmuramate--L-alanine ligase {ECO:0000255|HAMAP-Rule:MF_00046};
DE            EC=6.3.2.8 {ECO:0000255|HAMAP-Rule:MF_00046};
DE   AltName: Full=UDP-N-acetylmuramoyl-L-alanine synthetase {ECO:0000255|HAMAP-Rule:MF_00046};
GN   Name=murC {ECO:0000255|HAMAP-Rule:MF_00046};
GN   OrderedLocusNames=SbBS512_E0084;
OS   Shigella boydii serotype 18 (strain CDC 3083-94 / BS512).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=344609;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 3083-94 / BS512;
RA   Rasko D.A., Rosovitz M., Maurelli A.T., Myers G., Seshadri R., Cer R.,
RA   Jiang L., Ravel J., Sebastian Y.;
RT   "Complete sequence of Shigella boydii serotype 18 strain BS512.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00046}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) +
CC         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:0000255|HAMAP-Rule:MF_00046};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00046}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00046}.
CC   -!- SIMILARITY: Belongs to the MurCDEF family. {ECO:0000255|HAMAP-
CC       Rule:MF_00046}.
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DR   EMBL; CP001063; ACD06935.1; -; Genomic_DNA.
DR   RefSeq; WP_001096043.1; NC_010658.1.
DR   AlphaFoldDB; B2U296; -.
DR   SMR; B2U296; -.
DR   STRING; 344609.SbBS512_E0084; -.
DR   EnsemblBacteria; ACD06935; ACD06935; SbBS512_E0084.
DR   KEGG; sbc:SbBS512_E0084; -.
DR   HOGENOM; CLU_028104_2_2_6; -.
DR   OMA; DITYQLR; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001030; 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;
KW   ATP-binding; Cell cycle; Cell division; Cell shape;
KW   Cell wall biogenesis/degradation; Cytoplasm; Ligase; Nucleotide-binding;
KW   Peptidoglycan synthesis.
FT   CHAIN           1..491
FT                   /note="UDP-N-acetylmuramate--L-alanine ligase"
FT                   /id="PRO_1000091137"
FT   BINDING         126..132
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00046"
SQ   SEQUENCE   491 AA;  53583 MW;  B96156817BD8A913 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 FLGTGRRFDF LGEFPLEPVN GKSGTAMLVD DYGHHPTEVD
     ATIKAARAGW PDKNLVMLFQ PHRFTRTRDL YDDFANVLTQ VDTLLMLEVY PAGEAPIPGA
     DSRSLCRTIR GRGKIDPILV PDPAQVAEML APVLTGNDLI LVQGAGNIGK IARSLAEIKL
     KPQTPEEEQH D
 
 
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