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Database: UniProt
Entry: B8G672_CHLAD
LinkDB: B8G672_CHLAD
Original site: B8G672_CHLAD 
ID   B8G672_CHLAD            Unreviewed;       474 AA.
AC   B8G672;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 59.
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   OrderedLocusNames=Cagg_2945 {ECO:0000313|EMBL:ACL25805.1};
OS   Chloroflexus aggregans (strain MD-66 / DSM 9485).
OC   Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Chloroflexineae;
OC   Chloroflexaceae; Chloroflexus.
OX   NCBI_TaxID=326427 {ECO:0000313|EMBL:ACL25805.1, ECO:0000313|Proteomes:UP000002508};
RN   [1] {ECO:0000313|Proteomes:UP000002508}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MD-66 / DSM 9485 {ECO:0000313|Proteomes:UP000002508};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Foster B., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Bryant D.A., Richardson P.;
RT   "Complete sequence of Chloroflexus aggregans DSM 9485.";
RL   Submitted (DEC-2008) 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}.
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DR   EMBL; CP001337; ACL25805.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8G672; -.
DR   STRING; 326427.Cagg_2945; -.
DR   KEGG; cag:Cagg_2945; -.
DR   eggNOG; COG0769; Bacteria.
DR   HOGENOM; CLU_041534_0_0_0; -.
DR   OMA; WLWDVDY; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000002508; Chromosome.
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   CDD; cd16448; RING-H2; 1.
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};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_02214}.
FT   DOMAIN          66..226
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          343..455
FT                   /note="Lipid II isoglutaminyl synthase (glutamine-
FT                   hydrolyzing) subunit MurT C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08353"
FT   ACT_SITE        380
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"
FT   BINDING         226
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02214"
FT   BINDING         245
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02214"
FT   BINDING         248
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02214"
SQ   SEQUENCE   474 AA;  51084 MW;  922E11DB529B8C79 CRC64;
     MSTVTIYRMN HLRTTVALAL GRTARILSRR FHLGGGTSLP GQIARSIEPA ILTTICTALP
     DGVILIAGTN GKTTTSRMLA AILEHTGEPL LHNRAGANLL PGLTTVAITD TDWRGRPHAR
     RALFETDEAA LPQAIAETRP RLVVLLNLFR DQLDRYGEID TIAGNWRRAL QTLPETSTVV
     FNADDPAIAG LTEHLPARVI GFGLNDTRHA VAAATHIADS QFCQTCGHRY HYRHIFYAHI
     GHYTCPHCGR HRPDPQIALT TLEPRGLDGS ELQIRHPGGQ LQIHLPLPGL YNAQNALAAT
     AAALALGIAP ATIGVALTTF QAAFGRIERI TAGPNGPPML IALIKNPVGA SETVRMLTAT
     TTRPLHLLIA INDRFADGTD VSWLWDADFE PLAGRIARVT VSGTRAADMA LRLDYAGVDG
     AAITVIDDLP TALDTALATL PVGETLAVLP TYTAMLDLRA EIARRGWAKP FWET
//
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