ID A0A0R2KHV7_9LACO Unreviewed; 495 AA.
AC A0A0R2KHV7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=IV53_GL000947 {ECO:0000313|EMBL:KRN88976.1};
OS Ligilactobacillus ceti DSM 22408.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Ligilactobacillus.
OX NCBI_TaxID=1122146 {ECO:0000313|EMBL:KRN88976.1, ECO:0000313|Proteomes:UP000051500};
RN [1] {ECO:0000313|EMBL:KRN88976.1, ECO:0000313|Proteomes:UP000051500}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22408 {ECO:0000313|EMBL:KRN88976.1,
RC ECO:0000313|Proteomes:UP000051500};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRN88976.1}.
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DR EMBL; JQBZ01000025; KRN88976.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2KHV7; -.
DR STRING; 1122146.IV53_GL000947; -.
DR PATRIC; fig|1122146.4.peg.982; -.
DR eggNOG; COG0769; Bacteria.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000051500; 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:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:InterPro.
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; IPR018109; Folylpolyglutamate_synth_CS.
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.
DR PROSITE; PS01011; FOLYLPOLYGLU_SYNT_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00208};
KW Cell cycle {ECO:0000256|HAMAP-Rule:MF_00208,
KW ECO:0000256|RuleBase:RU004135};
KW Cell division {ECO:0000256|HAMAP-Rule:MF_00208,
KW ECO:0000256|RuleBase:RU004135};
KW Cell shape {ECO:0000256|HAMAP-Rule:MF_00208,
KW ECO:0000256|RuleBase:RU004135};
KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00208,
KW ECO:0000256|RuleBase:RU004135};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00208};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_00208, ECO:0000313|EMBL:KRN88976.1};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00208};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00208};
KW Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00208,
KW ECO:0000256|RuleBase:RU004135};
KW Reference proteome {ECO:0000313|Proteomes:UP000051500}.
FT DOMAIN 113..315
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 336..418
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
FT BINDING 34
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 115..121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
FT BINDING 156
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 157..158
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 184
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 192
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 226
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
SQ SEQUENCE 495 AA; 55260 MW; E2B15F5D21F1C86D CRC64;
MDFMELSQLL LGLDYEINNE KDLQLDVNDI IYDSRKAQPE TLFLSIHGID LNGDDYVLDA
YERGCRIFIL EQELQDLPTD TTVVLVSDTR QALSKMSANF FGHPSKEMTV VGVTGTKGKT
TVANYIKKVL CGVGINAGVI GTMGIFYNDQ EIETINTTPE SYELNKTMRA MLDAGVTAVA
MEVSSGGLMM NRVDDIDFDI GIFTNLSLDH IGPREHPTFE HYRDCKSRLF NLCKYGIINA
DDEYAEYMIE HATCPTTTYS VHHASDYQAH DIQLTRDGWH LGVAFTYDHK GEKTQTHIST
PGEFSVLNAL AVLATTQYLG VPKDEILKTL SRVTIDGRVE VLPVLDDVTV VIDFAHNGIS
LENVLTTLLD YHPKHLICVF GSIGNRAIIR RKELGDVAAK YCDVAVLTAD NPDREDPQII
IDEIAESFVD SKCKVLKIAD RSEAMYEAMK LAQPGDMVVI AGKGHEKYQV IDGKHVFYDE
RAEVIKAAER VKKEK
//
