ID   MURC_DESAL              Reviewed;         456 AA.
AC   B8FBR7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 76.
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}; OrderedLocusNames=Dalk_3130;
OS   Desulfatibacillum aliphaticivorans.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC   Desulfobacteraceae; Desulfatibacillum.
OX   NCBI_TaxID=218208;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AK-01;
RX   PubMed=21651686; DOI=10.1111/j.1462-2920.2011.02516.x;
RA   Callaghan A.V., Morris B.E., Pereira I.A., McInerney M.J., Austin R.N.,
RA   Groves J.T., Kukor J.J., Suflita J.M., Young L.Y., Zylstra G.J., Wawrik B.;
RT   "The genome sequence of Desulfatibacillum alkenivorans AK-01: a blueprint
RT   for anaerobic alkane oxidation.";
RL   Environ. Microbiol. 14:101-113(2012).
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; CP001322; ACL04820.1; -; Genomic_DNA.
DR   RefSeq; WP_015947880.1; NC_011768.1.
DR   AlphaFoldDB; B8FBR7; -.
DR   SMR; B8FBR7; -.
DR   EnsemblBacteria; ACL04820; ACL04820; Dalk_3130.
DR   KEGG; dal:Dalk_3130; -.
DR   eggNOG; COG0773; Bacteria.
DR   HOGENOM; CLU_028104_2_2_7; -.
DR   OMA; DITYQLR; -.
DR   OrthoDB; 307881at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000739; 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; Reference proteome.
FT   CHAIN           1..456
FT                   /note="UDP-N-acetylmuramate--L-alanine ligase"
FT                   /id="PRO_1000116620"
FT   BINDING         112..118
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00046"
SQ   SEQUENCE   456 AA;  49697 MW;  B888949312F756F7 CRC64;
     MYRKKYSIHF VGIGGIGMSG IAELLLNLGY QVSGSDIKES DITQRLAKLG GTIYRGHRAE
     NVKGCDVVVV SSAIRQENPE TASAREQGIP VIPRAEMLAE LMRLKYSVAI AGAHGKTTTT
     SIVADVLAAG GLDPTVVIGG KLLSIGSNAK LGHGEFIVAE ADESDGSFLK MSPSIAVVTN
     IDREHMDHYK DMDEIKDAFA QFVDKIPFYG LSVLCLDSEP VQDLIPFINK RYVTYGLTTQ
     ADLQAGDVTT EGLTSRFTVR HNKKRLGRIT LNLPGLHNVY NSLASIAVGL ELNVPFENIK
     AALESLSGVH RRLETKGKVG GIVVMDDYGH HPTEIRTTLQ AVNDSYPERR VGVIFQPHRY
     SRTQSLFEDF ARSFYQADYL VVLPIYPAGE KPIPGVDSVS LCKALKAYGH KHVIHAPSKE
     SALQELDKTV REGDVLITLG AGDVYRVGES FLASRS