ID   MURC_SYNE7              Reviewed;         478 AA.
AC   P95836; Q31ME8;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 2.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=UDP-N-acetylmuramate--L-alanine ligase;
DE            EC=6.3.2.8;
DE   AltName: Full=UDP-N-acetylmuramoyl-L-alanine synthetase;
GN   Name=murC; OrderedLocusNames=Synpcc7942_1741;
OS   Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS   R2).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX   NCBI_TaxID=1140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7942 / FACHB-805;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 199-478.
RA   Kirzner S., Kaplan A.;
RT   "Cyanobacterial mutants capable of growing in the presence of high
RT   concentration of zinc.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cell wall formation. {ECO:0000250}.
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   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MurCDEF family. {ECO:0000305}.
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DR   EMBL; CP000100; ABB57771.1; -; Genomic_DNA.
DR   EMBL; U86147; AAB47522.1; -; Genomic_DNA.
DR   RefSeq; WP_011244660.1; NC_007604.1.
DR   AlphaFoldDB; P95836; -.
DR   SMR; P95836; -.
DR   STRING; 1140.Synpcc7942_1741; -.
DR   PRIDE; P95836; -.
DR   EnsemblBacteria; ABB57771; ABB57771; Synpcc7942_1741.
DR   KEGG; syf:Synpcc7942_1741; -.
DR   eggNOG; COG0773; Bacteria.
DR   HOGENOM; CLU_028104_2_2_3; -.
DR   OMA; DITYQLR; -.
DR   OrthoDB; 307881at2; -.
DR   BioCyc; SYNEL:SYNPCC7942_1741-MON; -.
DR   UniPathway; UPA00219; -.
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..478
FT                   /note="UDP-N-acetylmuramate--L-alanine ligase"
FT                   /id="PRO_0000182174"
FT   CONFLICT        243
FT                   /note="L -> F (in Ref. 2; AAB47522)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        282
FT                   /note="L -> M (in Ref. 2; AAB47522)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   478 AA;  51605 MW;  395EF0CDD5FF1D8E CRC64;
     MTIAVDLQGR PFHFIGIGGI GMSALAQVVT ERQLPVSGSD IRRSHITDRL AQLGAQIFDR
     QAATNLEFFQ EAVSAGQSPQ VICSTAIHAH NEEYQAAIDL GCPVFHRSDL LAALLRVYES
     IAVAGTHGKT TTSGLIAYLL YQAGLDPTVV IGGEVNALGG NARLGQGRHL VAEADESDGS
     LVKLQAAIGI ITNIELDHPD HYCDLEAVIS TFKTFSDNCS QLIANWDCPT VRDRLPGTIS
     YSLDPARGAD YTVDQVSFRG SGTQARIWER GELLGRIHLP LLEAHNLSNA LAAIAACRHL
     GMDFASIREG LAGFEGARRR FEFRGSAQGI QFVDDYAHHP SELAATLAAA RLQIDSGCSR
     LPEVPKRLVA IFQPHRYSRT QAFLAEFAQS FGPADLVLIS DIYAAGERNP GQLSGQTLAD
     AIAQYQANVH YAPDLEAVEQ RLHQLLQPGD LALFLGAGNL NQVIPRLLDH YACDRSAA