ID H5U5C6_9ACTN Unreviewed; 440 AA.
AC H5U5C6;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=GOSPT_118_00100 {ECO:0000313|EMBL:GAB40934.1};
OS Gordonia sputi NBRC 100414.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1089453 {ECO:0000313|EMBL:GAB40934.1, ECO:0000313|Proteomes:UP000005845};
RN [1] {ECO:0000313|EMBL:GAB40934.1, ECO:0000313|Proteomes:UP000005845}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 100414 {ECO:0000313|EMBL:GAB40934.1,
RC ECO:0000313|Proteomes:UP000005845};
RA Yoshida I., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S.,
RA Fujita N.;
RT "Whole genome shotgun sequence of Gordonia sputi NBRC 100414.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:GAB40934.1}.
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DR EMBL; BAFC01000116; GAB40934.1; -; Genomic_DNA.
DR RefSeq; WP_005208024.1; NZ_BAFC01000116.1.
DR AlphaFoldDB; H5U5C6; -.
DR eggNOG; COG0769; Bacteria.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000005845; 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:0046872; F:metal ion binding; 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; 3.40.1190.10; 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};
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}.
FT DOMAIN 69..184
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 324..422
FT /note="Lipid II isoglutaminyl synthase (glutamine-
FT hydrolyzing) subunit MurT C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08353"
FT ACT_SITE 358
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02214"
SQ SEQUENCE 440 AA; 46202 MW; 686897621410B303 CRC64;
MPDRVPAPGG STTRVPVRTS LALGAASAAR WASRTAGRGK GSMIGGLVAE KIDPNIMGRL
AAGKRTALIT GTNGKSTTTR MTAAALAELG EVATQADGAN MDAGIIATLS LQRSAPVAAL
EVDELHVPHV SDAVDPEVVV MLNLSRDQLD RVGEINMIER RLREGLARHP DTTVIANCDD
VLITSAAFDA PKVVWVAAGA SWVGDSVSCP RTGEPIARTS GDPTDPSIQS GVDWYSTGDP
TFRRPTPQWW VDDEKIYGPD GFEASMTLSV PGRANRGNAA QAIAAAVAMG ADPAKAVAAV
STVGEVAGRY GIHQVGNHSV RTLLAKNPAG WQEALSMIDQ DADGLVIAVN GQVPDGEDLS
WLWDVRFEAF ETMQVVAAGE RAADLSVRLL YAGAEHTTIP DTMEAIASCP PGRVEVLANY
TAFRDLGVAI ERAERARKGQ
//
