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Database: UniProt
Entry: Q03Y77_LEUMM
LinkDB: Q03Y77_LEUMM
Original site: Q03Y77_LEUMM 
ID   Q03Y77_LEUMM            Unreviewed;       490 AA.
AC   Q03Y77;
DT   14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   14-NOV-2006, sequence version 1.
DT   27-MAR-2024, entry version 116.
DE   SubName: Full=UDP-N-acetylmuramyl tripeptide synthase {ECO:0000313|EMBL:ABJ61845.1};
GN   OrderedLocusNames=LEUM_0735 {ECO:0000313|EMBL:ABJ61845.1};
OS   Leuconostoc mesenteroides subsp. mesenteroides (strain ATCC 8293 / DSM
OS   20343 / BCRC 11652 / CCM 1803 / JCM 6124 / NCDO 523 / NBRC 100496 / NCIMB
OS   8023 / NCTC 12954 / NRRL B-1118 / 37Y).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Leuconostoc.
OX   NCBI_TaxID=203120 {ECO:0000313|EMBL:ABJ61845.1, ECO:0000313|Proteomes:UP000000362};
RN   [1] {ECO:0000313|EMBL:ABJ61845.1, ECO:0000313|Proteomes:UP000000362}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8293 / DSM 20343 / BCRC 11652 / CCM 1803 / JCM 6124 / NCDO
RC   523 / NBRC 100496 / NCIMB 8023 / NCTC 12954 / NRRL B-1118 / 37Y
RC   {ECO:0000313|Proteomes:UP000000362};
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K., Slesarev A., Wolf Y., Sorokin A., Mirkin B., Koonin E.,
RA   Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA   Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA   Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA   Baldwin K., Lee J.H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA   Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA   Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J., Hutkins R.,
RA   O'Sullivan D., Steele J., Unlu G., Saier M., Klaenhammer T., Richardson P.,
RA   Kozyavkin S., Weimer B., Mills D.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752, ECO:0000256|RuleBase:RU004135}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU004135}.
CC   -!- SIMILARITY: Belongs to the MurCDEF family. MurE subfamily.
CC       {ECO:0000256|ARBA:ARBA00005898}.
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DR   EMBL; CP000414; ABJ61845.1; -; Genomic_DNA.
DR   RefSeq; WP_011679524.1; NC_008531.1.
DR   AlphaFoldDB; Q03Y77; -.
DR   EnsemblBacteria; ABJ61845; ABJ61845; LEUM_0735.
DR   KEGG; lme:LEUM_0735; -.
DR   eggNOG; COG0769; Bacteria.
DR   HOGENOM; CLU_022291_4_2_9; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000362; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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-UniPathway.
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; 3.40.1390.10; MurE/MurF, N-terminal domain; 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; IPR035911; MurE/MurF_N.
DR   InterPro; IPR005761; UDP-N-AcMur-Glu-dNH2Pim_ligase.
DR   NCBIfam; TIGR01085; murE; 1.
DR   PANTHER; PTHR23135; MUR LIGASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR23135:SF4; UDP-N-ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE--2,6-DIAMINOPIMELATE LIGASE MURE HOMOLOG, CHLOROPLASTIC; 1.
DR   Pfam; PF02875; Mur_ligase_C; 1.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR   SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
DR   SUPFAM; SSF63418; MurE/MurF N-terminal domain; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cell cycle {ECO:0000256|RuleBase:RU004135};
KW   Cell division {ECO:0000256|RuleBase:RU004135};
KW   Cell shape {ECO:0000256|RuleBase:RU004135};
KW   Cell wall biogenesis/degradation {ECO:0000256|RuleBase:RU004135};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Peptidoglycan synthesis {ECO:0000256|RuleBase:RU004135}.
FT   DOMAIN          107..309
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          329..413
FT                   /note="Mur ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02875"
SQ   SEQUENCE   490 AA;  55048 MW;  2176F26EC7A1D8C8 CRC64;
     MRLTTETIQN LLVDHNLLLD APDVDMTFDF LHYDTREVQK NTLFVIKGAF KRAYLDNVHG
     ITGLITETKI DVDLPQWQVT NVQKALSLLS MAFFDYPQEQ LWIGAFTGTK GKTTAAYFAY
     TMLKEATNNH TALFSTVDRI TGPQASDKKK SDLTTPESYE LFKDMRQVVD NGMTHLVMEV
     SSQAYLKNRV YGLRYDVGAF LNISPDHIGP NEHPTFEDYL AHKLMLLDHS DEVIVNAETD
     HFDTIYTYAK KAHHKVYTYS RQMFTSEESA IHESRFTVVK SEFNEMLGSY RLNVPGDFNE
     SNAMAAMMLV SFAGVKHQAM VKGLDEVFIP GRMLSLPING HGVAFVDYAH NFVSMQALLS
     FAQAQYPNGR VLVVVGSPGN KGVSRRADFG HVVSDLADVV YLTADDPQFE NPLDIAHEIA
     AHINNDKLEV HYEMNRIAAI HEAISAANEN DIVIVAGKGE DPYQKIDGVD VPYIGDYAVV
     KQFRDQIKNP
//
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