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Database: UniProt
Entry: A0A1V2A7M5_9BACI
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ID   A0A1V2A7M5_9BACI        Unreviewed;       488 AA.
AC   A0A1V2A7M5;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=UDP-N-acetylmuramyl-tripeptide synthetase {ECO:0000256|HAMAP-Rule:MF_00208};
DE            EC=6.3.2.- {ECO:0000256|HAMAP-Rule:MF_00208};
DE   AltName: Full=UDP-MurNAc-tripeptide synthetase {ECO:0000256|HAMAP-Rule:MF_00208};
GN   Name=murE {ECO:0000256|HAMAP-Rule:MF_00208};
GN   ORFNames=BTO28_09420 {ECO:0000313|EMBL:OMP66947.1};
OS   Domibacillus epiphyticus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Domibacillus.
OX   NCBI_TaxID=1714355 {ECO:0000313|EMBL:OMP66947.1, ECO:0000313|Proteomes:UP000188613};
RN   [1] {ECO:0000313|EMBL:OMP66947.1, ECO:0000313|Proteomes:UP000188613}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAB 38 {ECO:0000313|EMBL:OMP66947.1,
RC   ECO:0000313|Proteomes:UP000188613};
RA   Verma A., Ojha A.K., Krishnamurthi S.;
RT   "Domibacillus sp. SAB 38T whole genome sequencing.";
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the addition of an amino acid to the nucleotide
CC       precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the
CC       biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000256|HAMAP-
CC       Rule:MF_00208}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00208};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752, ECO:0000256|HAMAP-Rule:MF_00208,
CC       ECO:0000256|RuleBase:RU004135}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00208,
CC       ECO:0000256|RuleBase:RU004135}.
CC   -!- PTM: Carboxylation is probably crucial for Mg(2+) binding and,
CC       consequently, for the gamma-phosphate positioning of ATP.
CC       {ECO:0000256|HAMAP-Rule:MF_00208}.
CC   -!- SIMILARITY: Belongs to the MurCDEF family. MurE subfamily.
CC       {ECO:0000256|ARBA:ARBA00005898, ECO:0000256|HAMAP-Rule:MF_00208}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00208}.
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:OMP66947.1}.
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DR   EMBL; MSFI01000013; OMP66947.1; -; Genomic_DNA.
DR   RefSeq; WP_076765614.1; NZ_MSFI01000013.1.
DR   AlphaFoldDB; A0A1V2A7M5; -.
DR   STRING; 1714355.BTO28_09420; -.
DR   OrthoDB; 9800958at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000188613; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016881; F:acid-amino acid ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; 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; 3.40.1390.10; MurE/MurF, N-terminal domain; 1.
DR   HAMAP; MF_00208; MurE; 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; 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; PF01225; Mur_ligase; 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|HAMAP-Rule:MF_00208};
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW   Rule:MF_00208};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW   Rule:MF_00208};
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW   Rule:MF_00208};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW   ECO:0000256|HAMAP-Rule:MF_00208};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00208};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00208, ECO:0000313|EMBL:OMP66947.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00208};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00208};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP-
KW   Rule:MF_00208}; Reference proteome {ECO:0000313|Proteomes:UP000188613}.
FT   DOMAIN          22..95
FT                   /note="Mur ligase N-terminal catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01225"
FT   DOMAIN          107..305
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          327..402
FT                   /note="Mur ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02875"
FT   BINDING         30
FT                   /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT                   glutamate"
FT                   /ligand_id="ChEBI:CHEBI:83900"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
FT   BINDING         109..115
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
FT   BINDING         150
FT                   /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT                   glutamate"
FT                   /ligand_id="ChEBI:CHEBI:83900"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
FT   BINDING         151..152
FT                   /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT                   glutamate"
FT                   /ligand_id="ChEBI:CHEBI:83900"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
FT   BINDING         175
FT                   /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT                   glutamate"
FT                   /ligand_id="ChEBI:CHEBI:83900"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
FT   BINDING         181
FT                   /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT                   glutamate"
FT                   /ligand_id="ChEBI:CHEBI:83900"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
FT   BINDING         183
FT                   /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT                   glutamate"
FT                   /ligand_id="ChEBI:CHEBI:83900"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
FT   MOD_RES         215
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
SQ   SEQUENCE   488 AA;  55163 MW;  DEEB844FA73B519B CRC64;
     MKLHTLLENV TNTMNESFRH IEIEGISTNS ASVRANELFV AIPGYTVDGH EFIRDAIKNG
     TIAIVGEKDM EDLAVPYIKV ASSRKALAEI ASQFYGNPSR KHTIIGITGT NGKTTTAFML
     KHILESNNLT CSLFGSVMNI VNGQISPSVN TTLDALELQR QLSLSHDDII IMEVSSHGLT
     QYRVQGIEFD YCLFTNLDQD HLDYHRHMDE YFAVKARLFD QLKPGGKAII NVYNSWGKKL
     YNQLQQKSID IFTLGDEEHH DLRIGKYIPS VVNSAEIYEG KIGAKLNLLL LGKHNIFNAS
     MAYLTARKLG IKKNTSILQA LETFHGVPGR FELFHHPKGA VFVVDYAHTA NALINCLQTA
     REYGANRIFH IFGFRGNRDK KKRKEMVRVS HKISDLTILT LDDLNDVPIQ EMERDLYVLN
     QQYGMVIPDR TLAIKHAWEQ VQEGDWVMIT GKGSETYQQP FQIPTNSDKE TLLYLNESRT
     TSKTLTVL
//
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