ID A0A0R2DDJ2_9LACO Unreviewed; 450 AA.
AC A0A0R2DDJ2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit MurT {ECO:0000256|HAMAP-Rule:MF_02214};
DE EC=6.3.5.13 {ECO:0000256|HAMAP-Rule:MF_02214};
GN Name=murT {ECO:0000256|HAMAP-Rule:MF_02214};
GN ORFNames=FC24_GL001197 {ECO:0000313|EMBL:KRM98603.1};
OS Loigolactobacillus rennini DSM 20253.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Loigolactobacillus.
OX NCBI_TaxID=1423796 {ECO:0000313|EMBL:KRM98603.1, ECO:0000313|Proteomes:UP000051638};
RN [1] {ECO:0000313|EMBL:KRM98603.1, ECO:0000313|Proteomes:UP000051638}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20253 {ECO:0000313|EMBL:KRM98603.1,
RC ECO:0000313|Proteomes:UP000051638};
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: The lipid II isoglutaminyl synthase complex catalyzes the
CC formation of alpha-D-isoglutamine in the cell wall lipid II stem
CC peptide. The MurT subunit catalyzes the ATP-dependent amidation of D-
CC glutamate residue of lipid II, converting it to an isoglutamine
CC residue. {ECO:0000256|HAMAP-Rule:MF_02214}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-
CC D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate + H2O + L-
CC glutamine = ADP + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-D-
CC isoglutaminyl-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl
CC diphosphate + H(+) + L-glutamate + phosphate; Xref=Rhea:RHEA:57928,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359,
CC ChEBI:CHEBI:60033, ChEBI:CHEBI:62233, ChEBI:CHEBI:456216;
CC EC=6.3.5.13; Evidence={ECO:0000256|HAMAP-Rule:MF_02214};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-
CC D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = ADP + beta-
CC D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-O-P-Glu-L-Lys-D-Ala-D-Ala)-
CC di-trans,octa-cis-undecaprenyl diphosphate; Xref=Rhea:RHEA:59488,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:60033, ChEBI:CHEBI:143132,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000256|HAMAP-Rule:MF_02214};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-O-P-Glu-L-Lys-D-
CC Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate + NH4(+) =
CC beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-D-isoglutaminyl-L-Lys-D-Ala-D-
CC Ala)-di-trans,octa-cis-undecaprenyl diphosphate + H(+) + phosphate;
CC Xref=Rhea:RHEA:57932, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:62233, ChEBI:CHEBI:143132;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02214};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752, ECO:0000256|HAMAP-Rule:MF_02214}.
CC -!- SUBUNIT: Forms a heterodimer with GatD. {ECO:0000256|HAMAP-
CC Rule:MF_02214}.
CC -!- SIMILARITY: Belongs to the MurCDEF family. MurT subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_02214}.
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:KRM98603.1}.
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DR EMBL; AYYI01000030; KRM98603.1; -; Genomic_DNA.
DR RefSeq; WP_057873767.1; NZ_AYYI01000030.1.
DR AlphaFoldDB; A0A0R2DDJ2; -.
DR STRING; 1423796.FC24_GL001197; -.
DR PATRIC; fig|1423796.3.peg.1222; -.
DR OrthoDB; 9803907at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000051638; Unassembled WGS sequence.
DR GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140282; F:carbon-nitrogen ligase activity on lipid II; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
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; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR HAMAP; MF_02214; Lipid_II_synth_MurT; 1.
DR InterPro; IPR043703; Lipid_II_synth_MurT.
DR InterPro; IPR036565; Mur-like_cat_sf.
DR InterPro; IPR013221; Mur_ligase_cen.
DR InterPro; IPR013564; MurT_C.
DR PANTHER; PTHR23135:SF7; LIPID II ISOGLUTAMINYL SYNTHASE (GLUTAMINE-HYDROLYZING) SUBUNIT MURT; 1.
DR PANTHER; PTHR23135; MUR LIGASE FAMILY MEMBER; 1.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR Pfam; PF08353; MurT_C; 1.
DR SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_02214}; Cell shape {ECO:0000256|HAMAP-Rule:MF_02214};
KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_02214};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_02214};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_02214};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02214};
KW Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_02214};
KW Reference proteome {ECO:0000313|Proteomes:UP000051638};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_02214}.
FT DOMAIN 54..202
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 320..429
FT /note="Lipid II isoglutaminyl synthase (glutamine-
FT hydrolyzing) subunit MurT C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08353"
FT ACT_SITE 356
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02214"
FT BINDING 206
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02214"
FT BINDING 209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02214"
FT BINDING 228
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02214"
FT BINDING 231
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02214"
SQ SEQUENCE 450 AA; 49808 MW; 394396A04DC45E52 CRC64;
MSVKSSFAVA VGRSSYWFLH TFMKGGSSLP GKLTNQIDPD ILATLGRDYE VVIITGTNGK
TLTTALTVKV LQAKYHNILT NPTGSNMKQG IITAFLTHKT GRSGKKIAVL EVDEANVIEV
TKYIKPTAFV FTNIFRDQMD RYGELYTTYK KILAGVAKAP DATIIANGDA PIFNSQSLPN
PIIYYGFNHQ QDGERKAPYN TDGVLCPVCN HILHYKFLIY SNLGKYYCPH CGFSRPKLQH
SVTALTHLTP TQSQFVVDQQ ALKINIGGTY NIYNALAAYS VGRYFDIAPD KIAQALDADE
KVFGRQEVIQ VGTKAVTLIL VKNPVGLNQV FNLISLNHKP FSLVTLLNAN YADGIDTSWI
WDSDFEKMAA QKLPCYIAGG ERVTDIAFRW QVAGVPKDSL IQIKDLDQVA EKIKNLPTQQ
VYVLATYTAV LQLREKLAAQ GFIAAANRKH
//
