MURT_STAAN
ID MURT_STAAN Reviewed; 437 AA.
AC A0A0H3JUU7;
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:0000255|HAMAP-Rule:MF_02214, ECO:0000269|PubMed:22291598, ECO:0000269|PubMed:30154570};
GN Name=murT {ECO:0000255|HAMAP-Rule:MF_02214, ECO:0000303|PubMed:22291598};
GN OrderedLocusNames=SA1708 {ECO:0000312|EMBL:BAB42978.1};
OS Staphylococcus aureus (strain N315).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N315;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY,
RP SUBUNIT, AND DISRUPTION PHENOTYPE.
RC STRAIN=N315;
RX PubMed=22291598; DOI=10.1371/journal.ppat.1002509;
RA Muench D., Roemer T., Lee S.H., Engeser M., Sahl H.G., Schneider T.;
RT "Identification and in vitro analysis of the GatD/MurT enzyme-complex
RT catalyzing lipid II amidation in Staphylococcus aureus.";
RL PLoS Pathog. 8:E1002509-E1002509(2012).
RN [3] {ECO:0007744|PDB:6GS2, ECO:0007744|PDB:6H5E}
RP X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) IN COMPLEXES WITH GATD AND ZINC,
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, DOMAIN, ACTIVE SITE, AND MUTAGENESIS
RP OF ASP-349.
RX PubMed=30154570; DOI=10.1038/s41598-018-31098-x;
RA Noldeke E.R., Muckenfuss L.M., Niemann V., Muller A., Stork E., Zocher G.,
RA Schneider T., Stehle T.;
RT "Structural basis of cell wall peptidoglycan amidation by the GatD/MurT
RT complex of Staphylococcus aureus.";
RL Sci. Rep. 8:12953-12953(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:22291598, PubMed:30154570). The MurT subunit catalyzes
CC the ATP-dependent amidation of D-glutamate residue of lipid II,
CC converting it to an isoglutamine residue (PubMed:22291598).
CC {ECO:0000269|PubMed:22291598, ECO:0000269|PubMed:30154570}.
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:0000255|HAMAP-Rule:MF_02214,
CC ECO:0000269|PubMed:22291598, ECO:0000269|PubMed:30154570};
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:0000255|HAMAP-Rule:MF_02214,
CC ECO:0000269|PubMed:22291598};
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:0000255|HAMAP-Rule:MF_02214,
CC ECO:0000269|PubMed:22291598};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5-7.8 for isoglutaminyl synthase activity.
CC {ECO:0000269|PubMed:22291598};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_02214, ECO:0000269|PubMed:22291598}.
CC -!- SUBUNIT: Forms a heterodimer with GatD. {ECO:0000255|HAMAP-
CC Rule:MF_02214, ECO:0000269|PubMed:22291598,
CC ECO:0000269|PubMed:30154570}.
CC -!- DOMAIN: Composed of two domains: a Mur ligase middle domain containing
CC the canonical ATP binding site and a ribbon-type zinc finger, and a C-
CC terminal Mur ligase domain. The GatD/MurT complex has an open,
CC boomerang-shaped conformation in which GatD is docked onto one end of
CC MurT. Both proteins contribute to the catalytic triad.
CC {ECO:0000269|PubMed:30154570}.
CC -!- DISRUPTION PHENOTYPE: The gatD-murT double mutant displays
CC susceptibility to diverse carbapenem and cephalosporin beta-lactam
CC antibiotics and shows increased susceptibility to plectasin.
CC {ECO:0000269|PubMed:22291598}.
CC -!- SIMILARITY: Belongs to the MurCDEF family. MurT subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_02214, ECO:0000305}.
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DR EMBL; BA000018; BAB42978.1; -; Genomic_DNA.
DR RefSeq; WP_001250343.1; NC_002745.2.
DR PDB; 6GS2; X-ray; 2.04 A; B/D=1-437.
DR PDB; 6H5E; X-ray; 2.14 A; B/D=1-437.
DR PDBsum; 6GS2; -.
DR PDBsum; 6H5E; -.
DR AlphaFoldDB; A0A0H3JUU7; -.
DR SMR; A0A0H3JUU7; -.
DR EnsemblBacteria; BAB42978; BAB42978; BAB42978.
DR KEGG; sau:SA1708; -.
DR HOGENOM; CLU_041534_0_0_9; -.
DR OMA; WLWDVDY; -.
DR BRENDA; 6.3.5.13; 3352.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000751; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140282; F:carbon-nitrogen ligase activity on lipid II; IDA:CACAO.
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 3D-structure; ATP-binding; Cell shape; Cell wall biogenesis/degradation;
KW Ligase; 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_0000446944"
FT ACT_SITE 349
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02214,
FT ECO:0000305|PubMed:30154570"
FT BINDING 202
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02214,
FT ECO:0000269|PubMed:30154570"
FT BINDING 205
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02214,
FT ECO:0000269|PubMed:30154570"
FT BINDING 224
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02214,
FT ECO:0000269|PubMed:30154570"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02214,
FT ECO:0000269|PubMed:30154570"
FT MUTAGEN 349
FT /note="D->N: Severe decrease in amidation of lipid II."
FT /evidence="ECO:0000269|PubMed:30154570"
FT HELIX 39..45
FT /evidence="ECO:0007829|PDB:6GS2"
FT STRAND 48..58
FT /evidence="ECO:0007829|PDB:6GS2"
FT HELIX 59..71
FT /evidence="ECO:0007829|PDB:6GS2"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:6GS2"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:6GS2"
FT HELIX 87..97
FT /evidence="ECO:0007829|PDB:6GS2"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:6GS2"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:6GS2"
FT HELIX 114..118
FT /evidence="ECO:0007829|PDB:6GS2"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:6GS2"
FT HELIX 141..153
FT /evidence="ECO:0007829|PDB:6GS2"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:6GS2"
FT HELIX 167..170
FT /evidence="ECO:0007829|PDB:6GS2"
FT HELIX 171..175
FT /evidence="ECO:0007829|PDB:6GS2"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:6GS2"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:6GS2"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:6GS2"
FT STRAND 211..216
FT /evidence="ECO:0007829|PDB:6GS2"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:6GS2"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:6H5E"
FT STRAND 234..250
FT /evidence="ECO:0007829|PDB:6GS2"
FT STRAND 253..256
FT /evidence="ECO:0007829|PDB:6GS2"
FT HELIX 264..277
FT /evidence="ECO:0007829|PDB:6GS2"
FT HELIX 282..289
FT /evidence="ECO:0007829|PDB:6GS2"
FT STRAND 295..304
FT /evidence="ECO:0007829|PDB:6GS2"
FT STRAND 307..311
FT /evidence="ECO:0007829|PDB:6GS2"
FT HELIX 317..328
FT /evidence="ECO:0007829|PDB:6GS2"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:6GS2"
FT STRAND 334..339
FT /evidence="ECO:0007829|PDB:6GS2"
FT TURN 344..346
FT /evidence="ECO:0007829|PDB:6GS2"
FT HELIX 351..354
FT /evidence="ECO:0007829|PDB:6GS2"
FT HELIX 358..363
FT /evidence="ECO:0007829|PDB:6GS2"
FT STRAND 366..373
FT /evidence="ECO:0007829|PDB:6GS2"
FT HELIX 376..385
FT /evidence="ECO:0007829|PDB:6GS2"
FT STRAND 392..394
FT /evidence="ECO:0007829|PDB:6GS2"
FT HELIX 398..404
FT /evidence="ECO:0007829|PDB:6GS2"
FT HELIX 405..407
FT /evidence="ECO:0007829|PDB:6GS2"
FT STRAND 408..416
FT /evidence="ECO:0007829|PDB:6GS2"
FT HELIX 418..420
FT /evidence="ECO:0007829|PDB:6GS2"
FT HELIX 421..432
FT /evidence="ECO:0007829|PDB:6GS2"
SQ SEQUENCE 437 AA; 49192 MW; C76BBEB0A67FE543 CRC64;
MRQWTAIHLA KLARKASRAV GKRGTDLPGQ IARKVDTDVL 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
