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Database: UniProt
Entry: A0A0G9FBV0_LACPN
LinkDB: A0A0G9FBV0_LACPN
Original site: A0A0G9FBV0_LACPN 
ID   A0A0G9FBV0_LACPN        Unreviewed;       436 AA.
AC   A0A0G9FBV0;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 67.
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   ECO:0000313|EMBL:ODO61455.1};
GN   ORFNames=ASV54_05980 {ECO:0000313|EMBL:APD00903.1}, AVR83_14640
GN   {ECO:0000313|EMBL:AOB24124.1}, C7M36_03056
GN   {ECO:0000313|EMBL:QHM38742.1}, C7M40_00831
GN   {ECO:0000313|EMBL:QHM48906.1}, Lp19_2888
GN   {ECO:0000313|EMBL:KZU91602.1}, LPJSA22_01433
GN   {ECO:0000313|EMBL:ODO61455.1};
OS   Lactiplantibacillus plantarum (Lactobacillus plantarum).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactiplantibacillus.
OX   NCBI_TaxID=1590 {ECO:0000313|EMBL:KZU91602.1, ECO:0000313|Proteomes:UP000076882};
RN   [1] {ECO:0000313|Proteomes:UP000183026}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MF1298 {ECO:0000313|Proteomes:UP000183026};
RA   McLeod A., Rud I., Axelsson L.;
RT   "Genome sequence of Lactobacillus plantarum MF1298, a candidate probiotic
RT   associated with unfavorable effect.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AOB24124.1, ECO:0000313|Proteomes:UP000093296}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DF {ECO:0000313|EMBL:AOB24124.1,
RC   ECO:0000313|Proteomes:UP000093296};
RA   Petkau K., Fast D., Duggal A., Foley E.;
RT   "Comparative evaluation of the genomes of common bacterial members of the
RT   Drosophila intestinal community.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:KZU91602.1, ECO:0000313|Proteomes:UP000076882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=19.1 {ECO:0000313|EMBL:KZU91602.1,
RC   ECO:0000313|Proteomes:UP000076882};
RA   Martino M.E.;
RT   "Comparative genomics of 54 Lactobacillus plantarum strains reveals genomic
RT   uncoupling from niche constraints.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:ODO61455.1, ECO:0000313|Proteomes:UP000094892}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JSA22 {ECO:0000313|EMBL:ODO61455.1,
RC   ECO:0000313|Proteomes:UP000094892};
RA   Choi H.S.;
RT   "Genome sequencing of Lactobacillus plantarum JSA22, isolated from
RT   fermented soybean paste.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EMBL:QHM38742.1, ECO:0000313|Proteomes:UP000464882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRCM101167 {ECO:0000313|EMBL:QHM38742.1,
RC   ECO:0000313|Proteomes:UP000464882};
RA   Jeong D.-Y.;
RT   "Lactobacillus plantatrum SRCM101167 having anti-virus activity species
RT   isolated from Korea kimchi.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [6] {ECO:0000313|EMBL:QHM48906.1, ECO:0000313|Proteomes:UP000465032}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRCM101518 {ECO:0000313|EMBL:QHM48906.1,
RC   ECO:0000313|Proteomes:UP000465032};
RA   Jeong D.-Y.;
RT   "Lactobacillus plantatrum SRCM101518 having antimicrbial activity species
RT   isolated from Korea kimchi.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [7] {ECO:0000313|EMBL:APD00903.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=MF1298 {ECO:0000313|EMBL:APD00903.1};
RA   McLeod A., Fagerlund A., Rud I., Axelsson L.;
RT   "Genome sequence of Lactobacillus plantarum MF1298, a candidate probiotic
RT   associated with unfavorable effect.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP013753; AOB24124.1; -; Genomic_DNA.
DR   EMBL; CP013149; APD00903.1; -; Genomic_DNA.
DR   EMBL; LUXM01000040; KZU91602.1; -; Genomic_DNA.
DR   EMBL; MCOL01000001; ODO61455.1; -; Genomic_DNA.
DR   EMBL; CP028334; QHM38742.1; -; Genomic_DNA.
DR   EMBL; CP028241; QHM48906.1; -; Genomic_DNA.
DR   RefSeq; WP_003640259.1; NZ_WWDG01000006.1.
DR   GeneID; 77217895; -.
DR   KEGG; lpb:SH83_06050; -.
DR   PATRIC; fig|1590.142.peg.1351; -.
DR   OMA; ELMRMKY; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000076882; Unassembled WGS sequence.
DR   Proteomes; UP000093296; Chromosome.
DR   Proteomes; UP000094892; Unassembled WGS sequence.
DR   Proteomes; UP000183026; Chromosome.
DR   Proteomes; UP000464882; Chromosome.
DR   Proteomes; UP000465032; 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; 3.90.190.20; 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          7..104
FT                   /note="Mur ligase N-terminal catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01225"
FT   DOMAIN          109..277
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          298..381
FT                   /note="Mur ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02875"
FT   BINDING         111..117
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00046"
SQ   SEQUENCE   436 AA;  48752 MW;  2BA58CDCF027287A CRC64;
     MDKATVYYFV GIKGSGMSSL ALILHDKGYQ VEGSDIEQYT FTQKGLAAAG IKMLPFSEDN
     IREGLTVIAG NSFTDDHPEI KKAREMGLPV YRYHEFLGKL MEGFTSIGVA GTHGKTSTTG
     LLSHVLSHIA PTSYLIGDGT GKGTPDARFF VFEADEYRRH FVAYHPDYAI MTNVDFDHPD
     YYKDLADVQS AFQQFGNQVK KGIFAWGDDE SLRHLDVDTP IYYYGTNDRD DFQAVNIKRT
     TKGSSFEVKY HDESLGEFEI PLFGEHNVLN STAVIAVSYF EKVNLDEIRR ELLDFSGVKR
     RFSEHQVGDM VMIDDYAHHP SEIKATLDAA RQKYPDKEIL AVFQPHTFSR TKALMDGFAA
     SLSKADHVFL TNIFSSAREK SGDVSSKDLA AKLPNGGEII TTDDMSALTA YHNAVAVFMG
     AGDIQKYEKI YEDQMK
//
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