ID A0A1Q5BV15_9ACTN Unreviewed; 415 AA.
AC A0A1Q5BV15;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=A6A27_18165 {ECO:0000313|EMBL:OKI75155.1};
OS Micromonospora sp. CB01531.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1718947 {ECO:0000313|EMBL:OKI75155.1, ECO:0000313|Proteomes:UP000186700};
RN [1] {ECO:0000313|EMBL:OKI75155.1, ECO:0000313|Proteomes:UP000186700}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB01531 {ECO:0000313|EMBL:OKI75155.1,
RC ECO:0000313|Proteomes:UP000186700};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(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:OKI75155.1}.
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DR EMBL; LWLS01000046; OKI75155.1; -; Genomic_DNA.
DR RefSeq; WP_073833908.1; NZ_LWLS01000046.1.
DR AlphaFoldDB; A0A1Q5BV15; -.
DR STRING; 1718947.A6A27_18165; -.
DR OrthoDB; 9803907at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000186700; 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|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, ECO:0000313|EMBL:OKI75155.1};
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:UP000186700};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_02214}.
FT DOMAIN 55..167
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 307..403
FT /note="Lipid II isoglutaminyl synthase (glutamine-
FT hydrolyzing) subunit MurT C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08353"
FT ACT_SITE 339
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02214"
FT BINDING 204
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02214"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02214"
FT BINDING 220
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02214"
FT BINDING 223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02214"
SQ SEQUENCE 415 AA; 44524 MW; C473BBE192AB718C CRC64;
MPMRAKVASS VSRTAAALSR AAGRGDGSVI GGWIGLKIDP DLLAHLSAGR AIALVSGTNG
KTTTTRLTAA AVGVLGRVAT NSFGANMPTG HTSALAKAGS TPYAVLEVDE HYLAQVLEAT
DPHVVALLNL SRDQLDRAKE VAMMAQLWRA ALVRHPDVRV VANADDPMVV WAATPPADPA
QGHIPPKVTW FSAGQRWHDD SWVCPECGAT IQRSGDQWWC TGCPLRRPAP QWAVEDDGVL
DPTGAWHKIQ LQLPGRVNLG NAATALAVAA EFGVRPVDAV SRLGTVTSVA GRYAQVDRDG
RNIRLLLAKN PASWLEAFDM ADEAPTLLSI NARDPDGLDT SWLFDVDFAP LRGRQVLITG
DRAYDLAVRL DVNGVPFQHV RSFDEAVRAV PPGRLEVIAN YTAFQDIRAE LDRVN
//
