MURT_STAAC
ID MURT_STAAC Reviewed; 437 AA.
AC A0A0H2WZQ7;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit MurT {ECO:0000255|HAMAP-Rule:MF_02214, ECO:0000305};
DE EC=6.3.5.13 {ECO:0000250|UniProtKB:A0A0H3JUU7, ECO:0000255|HAMAP-Rule:MF_02214};
GN Name=murT {ECO:0000255|HAMAP-Rule:MF_02214, ECO:0000303|PubMed:22303291};
GN OrderedLocusNames=SACOL1951 {ECO:0000312|EMBL:AAW38392.1};
OS Staphylococcus aureus (strain COL).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93062;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
RN [2]
RP FUNCTION, PATHWAY, AND DISRUPTION PHENOTYPE.
RC STRAIN=COL;
RX PubMed=22303291; DOI=10.1371/journal.ppat.1002508;
RA Figueiredo T.A., Sobral R.G., Ludovice A.M., Almeida J.M., Bui N.K.,
RA Vollmer W., de Lencastre H., Tomasz A.;
RT "Identification of genetic determinants and enzymes involved with the
RT amidation of glutamic acid residues in the peptidoglycan of Staphylococcus
RT aureus.";
RL PLoS Pathog. 8:E1002508-E1002508(2012).
RN [3]
RP SUBUNIT.
RC STRAIN=COL;
RX PubMed=29593310; DOI=10.1038/s41598-018-22986-3;
RA Leisico F., Vieira D.V., Figueiredo T.A., Silva M., Cabrita E.J.,
RA Sobral R.G., Ludovice A.M., Trincao J., Romao M.J., de Lencastre H.,
RA Santos-Silva T.;
RT "First insights of peptidoglycan amidation in Gram-positive bacteria - the
RT high-resolution crystal structure of Staphylococcus aureus glutamine
RT amidotransferase GatD.";
RL Sci. Rep. 8:5313-5313(2018).
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 (PubMed:22303291). The MurT subunit catalyzes the ATP-dependent
CC amidation of D-glutamate residue of lipid II, converting it to an
CC isoglutamine residue (By similarity).
CC {ECO:0000250|UniProtKB:A0A0H3JUU7, ECO:0000269|PubMed:22303291}.
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:0000250|UniProtKB:A0A0H3JUU7,
CC ECO:0000255|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:0000250|UniProtKB:A0A0H3JUU7,
CC ECO:0000255|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:0000250|UniProtKB:A0A0H3JUU7, ECO:0000255|HAMAP-
CC Rule:MF_02214};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_02214, ECO:0000269|PubMed:22303291}.
CC -!- SUBUNIT: Forms a heterodimer with GatD. {ECO:0000255|HAMAP-
CC Rule:MF_02214, ECO:0000269|PubMed:29593310}.
CC -!- DISRUPTION PHENOTYPE: The gatD-murT double mutant shows abnormal
CC peptidoglycan composition, with decreased amidation of the glutamate
CC residue. The mutant has a normal morphology but growth rate is greatly
CC reduced. Mutant shows reduced antibiotic resistance and increased
CC sensitivity to lysozyme. {ECO:0000269|PubMed:22303291}.
CC -!- SIMILARITY: Belongs to the MurCDEF family. MurT subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_02214, ECO:0000305}.
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DR EMBL; CP000046; AAW38392.1; -; Genomic_DNA.
DR RefSeq; WP_001250336.1; NC_002951.2.
DR AlphaFoldDB; A0A0H2WZQ7; -.
DR SMR; A0A0H2WZQ7; -.
DR EnsemblBacteria; AAW38392; AAW38392; SACOL1951.
DR KEGG; sac:SACOL1951; -.
DR HOGENOM; CLU_041534_0_0_9; -.
DR OMA; WLWDVDY; -.
DR BRENDA; 6.3.5.13; 3352.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000530; 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: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; -; 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 Pfam; PF08245; Mur_ligase_M; 1.
DR Pfam; PF08353; MurT_C; 1.
DR SUPFAM; SSF53623; SSF53623; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell shape; Cell wall biogenesis/degradation; Ligase;
KW Metal-binding; Nucleotide-binding; Peptidoglycan synthesis; Zinc.
FT CHAIN 1..437
FT /note="Lipid II isoglutaminyl synthase (glutamine-
FT hydrolyzing) subunit MurT"
FT /id="PRO_0000446943"
FT ACT_SITE 349
FT /evidence="ECO:0000250|UniProtKB:A0A0H3JUU7,
FT ECO:0000255|HAMAP-Rule:MF_02214"
FT BINDING 202
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:A0A0H3JUU7,
FT ECO:0000255|HAMAP-Rule:MF_02214"
FT BINDING 205
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:A0A0H3JUU7,
FT ECO:0000255|HAMAP-Rule:MF_02214"
FT BINDING 224
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:A0A0H3JUU7,
FT ECO:0000255|HAMAP-Rule:MF_02214"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:A0A0H3JUU7,
FT ECO:0000255|HAMAP-Rule:MF_02214"
SQ SEQUENCE 437 AA; 49206 MW; C9F5846440A63255 CRC64;
MRQWTAIHLA KLARKASRAV GKRGTDLPGQ IARKVDTDIL RKLAEQVDDI VFISGTNGKT
TTSNLIGHTL KANNIQIIHN NEGANMAAGI TSAFIMQSTP KTKIAVIEID EGSIPRVLKE
VTPSMMVFTN FFRDQMDRFG EIDIMVNNIA ETISNKGIKL LLNADDPFVS RLKIASDTIV
YYGMKAHAHE FEQSTMNESR YCPNCGRLLQ YDYIHYNQIG HYHCQCGFKR EQAKYEISSF
DVAPFLYLNI NDEKYDMKIA GDFNAYNALA AYTVLRELGL NEQTIKNGFE TYTSDNGRMQ
YFKKERKEAM INLAKNPAGM NASLSVGEQL EGEKVYVISL NDNAADGRDT SWIYDADFEK
LSKQQIEAII VTGTRAEELQ LRLKLAEVEV PIIVERDIYK ATAKTMDYKG FTVAIPNYTS
LAPMLEQLNR SFEGGQS
