ID A0A1F6HEB2_9BACT Unreviewed; 425 AA.
AC A0A1F6HEB2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 14.
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=A2152_03605 {ECO:0000313|EMBL:OGH08740.1};
OS Candidatus Levybacteria bacterium RBG_16_35_6.
OC Bacteria; Candidatus Levybacteria.
OX NCBI_TaxID=1798585 {ECO:0000313|EMBL:OGH08740.1, ECO:0000313|Proteomes:UP000176720};
RN [1] {ECO:0000313|EMBL:OGH08740.1, ECO:0000313|Proteomes:UP000176720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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|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:OGH08740.1}.
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DR EMBL; MFNI01000055; OGH08740.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6HEB2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000176720; Unassembled WGS sequence.
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:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:InterPro.
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; IPR018109; Folylpolyglutamate_synth_CS.
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.
DR PROSITE; PS01011; FOLYLPOLYGLU_SYNT_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_02214};
KW 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 Zinc {ECO:0000256|HAMAP-Rule:MF_02214}.
FT DOMAIN 54..194
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 305..412
FT /note="Lipid II isoglutaminyl synthase (glutamine-
FT hydrolyzing) subunit MurT C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08353"
FT ACT_SITE 340
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 212
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"
FT BINDING 234
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02214"
SQ SEQUENCE 425 AA; 47593 MW; BEC68CD239BB52F6 CRC64;
MLNFLIVLIG KSVSLFSNFF NLGSGGTWPG HIALKLNKNF IDQAIDSKTK IVLVAGTNGK
TSTATLITHI LTQCGNQVAH NKTGANQLNG IASAIISEIP KLSNKLIKDY LILEVDENVL
PLALKKLTPN TMICLNLFRD QLDRYGEIDS IVKKWRDSFS KLSTNTTLIL NADDPQMAIL
GTKKTKNYFF GLNLNLEKEI QHGADSIFCP NCQSELIYKT ISFSHLGNWA CPTCKLKRPS
LDISSSNFFP LAGTYGKYIT LAAILFAKNQ KISQEKILSS IKKFKPPFGR QEKFEINGKK
IEILLSKNPT SFNESLKTIK NQGAKNVLLV LNDHYVDGID VSWIWDIDFE NLLSKSTNIA
VSGERVYDIA IRLKYAEKFT HIFTDLDEAI NKMIENIAMG EKLYVLANYS AMLETRKILL
GRKLL
//
