ID T0UT31_LACLC Unreviewed; 443 AA.
AC T0UT31;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=UDP-N-acetylmuramate--L-alanine ligase {ECO:0000256|ARBA:ARBA00012211, ECO:0000256|HAMAP-Rule:MF_00046};
DE EC=6.3.2.8 {ECO:0000256|ARBA:ARBA00012211, ECO:0000256|HAMAP-Rule:MF_00046};
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 ORFNames=LLT1_03330 {ECO:0000313|EMBL:EQC88750.1};
OS Lactococcus cremoris subsp. cremoris TIFN1.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus; Lactococcus cremoris subsp. cremoris.
OX NCBI_TaxID=1234871 {ECO:0000313|EMBL:EQC88750.1, ECO:0000313|Proteomes:UP000015849};
RN [1] {ECO:0000313|EMBL:EQC88750.1, ECO:0000313|Proteomes:UP000015849}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TIFN1 {ECO:0000313|EMBL:EQC88750.1};
RX PubMed=23823494; DOI=10.1038/ismej.2013.108;
RA Erkus O., de Jager V.C., Spus M., van Alen-Boerrigter I.J.,
RA van Rijswijck I.M., Hazelwood L., Janssen P.W., van Hijum S.A.,
RA Kleerebezem M., Smid E.J.;
RT "Multifactorial diversity sustains microbial community stability.";
RL ISME J. 7:2126-2136(2013).
CC -!- FUNCTION: Cell wall formation. {ECO:0000256|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:0000256|ARBA:ARBA00001677, ECO:0000256|HAMAP-
CC Rule:MF_00046};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752, ECO:0000256|HAMAP-Rule:MF_00046}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00046}.
CC -!- SIMILARITY: Belongs to the MurCDEF family. {ECO:0000256|HAMAP-
CC Rule:MF_00046}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EQC88750.1}.
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DR EMBL; ASXF01000070; EQC88750.1; -; Genomic_DNA.
DR AlphaFoldDB; T0UT31; -.
DR PATRIC; fig|1234871.3.peg.416; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000015849; Unassembled WGS sequence.
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; 3.90.190.20; Mur ligase, C-terminal domain; 1.
DR Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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 NCBIfam; TIGR01082; murC; 1.
DR PANTHER; PTHR43445:SF3; UDP-N-ACETYLMURAMATE--L-ALANINE LIGASE; 1.
DR PANTHER; PTHR43445; UDP-N-ACETYLMURAMATE--L-ALANINE LIGASE-RELATED; 1.
DR Pfam; PF01225; Mur_ligase; 1.
DR Pfam; PF02875; Mur_ligase_C; 1.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR SUPFAM; SSF51984; MurCD N-terminal domain; 1.
DR SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00046};
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW Rule:MF_00046};
KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW Rule:MF_00046};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW Rule:MF_00046};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW ECO:0000256|HAMAP-Rule:MF_00046};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00046};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00046};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00046};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP-
KW Rule:MF_00046}.
FT DOMAIN 5..103
FT /note="Mur ligase N-terminal catalytic"
FT /evidence="ECO:0000259|Pfam:PF01225"
FT DOMAIN 108..277
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 297..378
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
FT BINDING 110..116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00046"
SQ SEQUENCE 443 AA; 50023 MW; BD88213F08AF84A3 CRC64;
MEKTYHFTGI KGSGMSALAL MLHQMGKNVQ GSDSTDYFFT QRGLEQVGVP LLPFDEKNIK
PEFELIVGNA FRDDNNVEIA FAHKNGFPFK RYHEFLGHFM EDFTSIGVAG AHGKTSTTGM
LAHVMSNIVD TSYLIGDGTG RGNAGSEYFV FESDEYERHF MPYHPEYTIM TNIDFDHPDY
FEGIEDVTSA FQDYANNIKK GIFAYGEDVN LRKLSAKAPI YYYGFEANDD YRAENLIRST
RGSSFDAYFR GEKIGHFVVP TYGKHNVLNA LSVVAVCHNL GLDMTDVADH LLTFRGVKRR
FTEKKVGETV IIDDFAHHPT EIEATLDAAR QKYPDREIVA VFQPHTFTRT IAFADEFAEV
LDHADTVYLA QIYGSAREVD HHEITAQDLA DKVRKPAKVI ELDNVSPLLD HDRGIYVFMG
AGNIQKYEIA FEKLLSQTST NLQ
//
