ID A0A0C5B9H5_9MICO Unreviewed; 520 AA.
AC A0A0C5B9H5;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 46.
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=C5C51_04750 {ECO:0000313|EMBL:PPI15120.1}, VT73_09460
GN {ECO:0000313|EMBL:KKM44711.1};
OS Rathayibacter toxicus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Rathayibacter.
OX NCBI_TaxID=145458 {ECO:0000313|EMBL:KKM44711.1, ECO:0000313|Proteomes:UP000052979};
RN [1] {ECO:0000313|EMBL:KKM44711.1, ECO:0000313|Proteomes:UP000052979}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FH142 {ECO:0000313|EMBL:KKM44711.1,
RC ECO:0000313|Proteomes:UP000052979};
RG Consortium for Microbial Forensics and Genomics (microFORGE);
RA Knight B.M., Roberts D.P., Lin D., Hari K., Fletcher J., Melcher U.,
RA Blagden T., Luster D.G., Sechler A.J., Schneider W.L., Winegar R.A.;
RT "Draft genome sequence of Rathayibacter toxicus strain FH-142 (AKA 70134 or
RT CS 32), a Western Australian isolate.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PPI15120.1, ECO:0000313|Proteomes:UP000237966}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FH99 {ECO:0000313|EMBL:PPI15120.1,
RC ECO:0000313|Proteomes:UP000237966};
RA Davis E.W.II., Tabima J.F., Weisberg A.J., Lopes L.D., Wiseman M.S.,
RA Wiseman M.S., Pupko T., Belcher M.S., Sechler A.J., Tancos M.A.,
RA Schroeder B.K., Murray T.D., Luster D.G., Schneider W.L., Rogers E.,
RA Andreote F.D., Grunwald N.J., Putnam M.L., Chang J.H.;
RT "Bacteriophage NCPPB3778 and a type I-E CRISPR drive the evolution of the
RT US Biological Select Agent, Rathayibacter toxicus.";
RL Submitted (FEB-2018) 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|HAMAP-Rule:MF_00208, 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:KKM44711.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LBFI01000053; KKM44711.1; -; Genomic_DNA.
DR EMBL; PSWU01000007; PPI15120.1; -; Genomic_DNA.
DR RefSeq; WP_027691967.1; NZ_PSXN01000009.1.
DR AlphaFoldDB; A0A0C5B9H5; -.
DR STRING; 145458.APU90_01495; -.
DR GeneID; 66874462; -.
DR KEGG; rtc:APU90_01495; -.
DR KEGG; rtx:TI83_04980; -.
DR PATRIC; fig|145458.7.peg.1149; -.
DR eggNOG; COG0769; Bacteria.
DR OrthoDB; 9800958at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000052979; Unassembled WGS sequence.
DR Proteomes; UP000237966; 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:PPI15120.1};
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:UP000052979}.
FT DOMAIN 39..109
FT /note="Mur ligase N-terminal catalytic"
FT /evidence="ECO:0000259|Pfam:PF01225"
FT DOMAIN 128..335
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 359..444
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
FT BINDING 45
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 47
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 130..136
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
FT BINDING 172..173
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 199
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 207
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 239
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
SQ SEQUENCE 520 AA; 55472 MW; 14F21BA187757D70 CRC64;
MHDTRPLSSL RPEHPVPRSL SQLIAEFALD SVQGAEGVEI RGITLDSHQV EAGDLYVGVA
GRRTHGAAFA SAAASSGAVA VLTDPEGAAL AADSGLPVLI TPDPRAALGD VAAWIYRTGE
NTSTLLGVTG TNGKTSVVYL LDALLRRLGV VSGLSSTAER RIGDVAVVSS LTTPEASELH
GLLARMQESA VRAVSIEVSA QALSRHRIDG LVFAVVGFTN LSHDHLDDYS DMEEYFEAKA
GLFEPERARR GVVTVDSVWG RRLAERSRIP VATLATSSVQ GLAPETPADW WMTVIEATAD
STTFRLDGPQ NRSVVVNVSL IGWYMAANTA LAIVMLVESG FDLDAITHAL DDSRLEVYIP
GRAELVSGER GPRVYVDYGH TPDAFSNALE ALRAITPGRV IMVFGADGDR DRTKRGAMGS
IAARLADVVI VTDFHPRWED PAAIRAALLT AATGAVPDRE IHEVPDPRSA VRAAIALARE
GDSILYAGPG HEDYQEIAGV HMPYSARDDV RQALREAGWL
//
