ID A0A0A7I8U7_9BIFI Unreviewed; 482 AA.
AC A0A0A7I8U7;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=AH67_00915 {ECO:0000313|EMBL:AIZ15670.1};
OS Bifidobacterium pseudolongum PV8-2.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1447715 {ECO:0000313|EMBL:AIZ15670.1, ECO:0000313|Proteomes:UP000030636};
RN [1] {ECO:0000313|EMBL:AIZ15670.1, ECO:0000313|Proteomes:UP000030636}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PV8-2 {ECO:0000313|EMBL:AIZ15670.1,
RC ECO:0000313|Proteomes:UP000030636};
RX PubMed=25614573;
RA Vazquez-Gutierrez P., Lacroix C., Chassard C., Klumpp J., Stevens M.J.,
RA Jans C.;
RT "Bifidobacterium pseudolongum Strain PV8-2, Isolated from a Stool Sample of
RT an Anemic Kenyan Infant.";
RL Genome Announc. 3:0-0(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|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}.
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DR EMBL; CP007457; AIZ15670.1; -; Genomic_DNA.
DR RefSeq; WP_039170929.1; NZ_CP007457.1.
DR AlphaFoldDB; A0A0A7I8U7; -.
DR STRING; 1447715.AH67_00915; -.
DR KEGG; bpsp:AH67_00915; -.
DR HOGENOM; CLU_041534_0_0_11; -.
DR OrthoDB; 9803907at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000030636; Chromosome.
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:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:InterPro.
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, ECO:0000313|EMBL:AIZ15670.1};
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:UP000030636}.
FT DOMAIN 68..286
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 357..462
FT /note="Lipid II isoglutaminyl synthase (glutamine-
FT hydrolyzing) subunit MurT C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08353"
FT ACT_SITE 391
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02214"
SQ SEQUENCE 482 AA; 51633 MW; F34AC9973E8F2323 CRC64;
MTQAPTGTPA PRAPWYAFAT PTLGKGVRWA SRITHHGGSA FPGKVVERVD PGFLRRTLAQ
LPLGVVLVSG TNGKTTTTRM VSMMLESLGL RVFTNPTGSN FTRGVVSALL QEVSAGGALD
ADIAVLELDE AYAVHFVEQV RPDYALLLNV MRDQLDRFGE IDNTARLLSR VAAATTGTVV
LNREDPRVAA LAQVVPSGTR TVHFGLSQAL RRFFPTDDDM ATTFERDAAP AVPAAEPTAG
TVADVMLTGV GDHRAQLLID GTEYDSEVRL EGVYNLYNAA AALAVVRAVQ ANVRNPQAIR
ERAARLPAKR RDGFVMRAQR FAGASTDALV DALAQVTPAF GRGEVIDVQG SPVELLLVKN
PMGFRLALAS FPPAGCNTMI CINDEYADGR DMSWLWDVDF TSLHATGVDA VSGVRAWDMA
LRLEYDGVAA RGVNTDLEQA VRAFVGMDPG TRKHIYCTYT AMLAVRSILG TMADVADAGV
GK
//
