MURC_PSET1
ID MURC_PSET1 Reviewed; 483 AA.
AC Q3IFY1;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 100.
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=PSHAa2503;
OS Pseudoalteromonas translucida (strain TAC 125).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=326442;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TAC 125;
RX PubMed=16169927; DOI=10.1101/gr.4126905;
RA Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G., Ho C.,
RA Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C., Rouy Z.,
RA Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT "Coping with cold: the genome of the versatile marine Antarctica bacterium
RT Pseudoalteromonas haloplanktis TAC125.";
RL Genome Res. 15:1325-1335(2005).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI87551.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CR954246; CAI87551.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041454564.1; NC_007481.1.
DR AlphaFoldDB; Q3IFY1; -.
DR SMR; Q3IFY1; -.
DR STRING; 326442.PSHAa2503; -.
DR EnsemblBacteria; CAI87551; CAI87551; PSHAa2503.
DR KEGG; pha:PSHAa2503; -.
DR PATRIC; fig|326442.8.peg.2413; -.
DR eggNOG; COG0773; Bacteria.
DR HOGENOM; CLU_028104_2_2_6; -.
DR OrthoDB; 307881at2; -.
DR BioCyc; PHAL326442:PSHA_RS12325-MON; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000006843; Chromosome I.
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..483
FT /note="UDP-N-acetylmuramate--L-alanine ligase"
FT /id="PRO_0000242575"
FT BINDING 125..131
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00046"
SQ SEQUENCE 483 AA; 52535 MW; 8F5B045F755DB35B CRC64;
MKQTSIREQY TRPAMRRIET IHFVGIGGAG MGGIAEVLAF EGYRITGSDI AHSAMTDRLI
KAGAEVFIGH HENNVKDANV VVVSSAIDET NPEIIAAKAA RVPVVRRAEM LAELMRFRHG
IAIAGTHGKT TTTSLIASIY AQAGLDPTFI IGGLLNSAGS NAKVGKSDFL IAEADESDAS
FLHLQPMVSV ITNIEEDHME TYGGSLEKMK DTYVDFIHNL PFYGLAVVCI DSEVASELIP
RFGRPVITYG ESSDADYRMS DFSQSANTCK FTVTNKQGES LTATLNMPGK HNALNATAAI
AVAKDQNIAN FAILEALQKF EGIGRRFQHY GEFENERGSV MLVDDYGHHP SEVAATITAA
REGWPDKRLV MVYQPHRFTR TRDLYEDFVK VLAEVDQLLL LDVYSAGEEP IVGADSKSLC
RSLRQRGKEP RHVANSAELA SVLADCLQNN DLVLTQGAGN IGQLVKTLAA TGMSIEKLKQ
GEV