MURT_STRR6
ID MURT_STRR6 Reviewed; 447 AA.
AC Q8DNZ9;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 96.
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:24044435, ECO:0000269|PubMed:30093673};
GN Name=murT {ECO:0000255|HAMAP-Rule:MF_02214, ECO:0000303|PubMed:24044435};
GN OrderedLocusNames=spr1443 {ECO:0000312|EMBL:AAL00247.1};
OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=171101;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL J. Bacteriol. 183:5709-5717(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=24044435; DOI=10.1021/cb400575t;
RA Zapun A., Philippe J., Abrahams K.A., Signor L., Roper D.I., Breukink E.,
RA Vernet T.;
RT "In vitro reconstitution of peptidoglycan assembly from the Gram-positive
RT pathogen Streptococcus pneumoniae.";
RL ACS Chem. Biol. 8:2688-2696(2013).
RN [3] {ECO:0007744|PDB:6FQB}
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) IN COMPLEX WITH GATD AND GLUTAMINE,
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF LYS-59; ASN-85; ASP-136; ASP-139;
RP ARG-140; GLU-143 AND ASP-355.
RX PubMed=30093673; DOI=10.1038/s41467-018-05602-w;
RA Morlot C., Straume D., Peters K., Hegnar O.A., Simon N., Villard A.M.,
RA Contreras-Martel C., Leisico F., Breukink E., Gravier-Pelletier C.,
RA Le Corre L., Vollmer W., Pietrancosta N., Havarstein L.S., Zapun A.;
RT "Structure of the essential peptidoglycan amidotransferase MurT/GatD
RT complex from Streptococcus pneumoniae.";
RL Nat. Commun. 9:3180-3180(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:24044435, PubMed:30093673). The MurT subunit catalyzes
CC the ATP-dependent amidation of D-glutamate residue of lipid II,
CC converting it to an isoglutamine residue (PubMed:30093673).
CC {ECO:0000269|PubMed:24044435, ECO:0000269|PubMed:30093673}.
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:24044435, ECO:0000269|PubMed:30093673};
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:30093673};
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:30093673};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=220 uM for lipid II {ECO:0000269|PubMed:30093673};
CC KM=16 uM for ATP {ECO:0000269|PubMed:30093673};
CC Note=kcat is 4 sec(-1) with lipid II as substrate.
CC {ECO:0000269|PubMed:30093673};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_02214, ECO:0000269|PubMed:24044435}.
CC -!- SUBUNIT: Forms a heterodimer with GatD. {ECO:0000255|HAMAP-
CC Rule:MF_02214, ECO:0000269|PubMed:30093673}.
CC -!- DISRUPTION PHENOTYPE: Severe depletion of GatD/MurT produces a high
CC proportion of aberrant cells, elongated or bulging.
CC {ECO:0000269|PubMed:30093673}.
CC -!- SIMILARITY: Belongs to the MurCDEF family. MurT subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_02214, ECO:0000305}.
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DR EMBL; AE007317; AAL00247.1; -; Genomic_DNA.
DR PIR; B98052; B98052.
DR RefSeq; NP_359036.1; NC_003098.1.
DR RefSeq; WP_001050251.1; NC_003098.1.
DR PDB; 6FQB; X-ray; 3.00 A; A/B/C/D=1-447.
DR PDBsum; 6FQB; -.
DR AlphaFoldDB; Q8DNZ9; -.
DR SMR; Q8DNZ9; -.
DR STRING; 171101.spr1443; -.
DR EnsemblBacteria; AAL00247; AAL00247; spr1443.
DR GeneID; 60234373; -.
DR KEGG; spr:spr1443; -.
DR PATRIC; fig|171101.6.peg.1559; -.
DR eggNOG; COG0770; Bacteria.
DR HOGENOM; CLU_041534_0_0_9; -.
DR OMA; WLWDVDY; -.
DR BRENDA; 6.3.5.13; 1960.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000586; 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 3D-structure; ATP-binding; Cell shape; Cell wall biogenesis/degradation;
KW Ligase; Metal-binding; Nucleotide-binding; Peptidoglycan synthesis;
KW Reference proteome; Zinc.
FT CHAIN 1..447
FT /note="Lipid II isoglutaminyl synthase (glutamine-
FT hydrolyzing) subunit MurT"
FT /id="PRO_0000446945"
FT ACT_SITE 355
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 208
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 227
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 230
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:A0A0H3JUU7,
FT ECO:0000255|HAMAP-Rule:MF_02214"
FT MUTAGEN 59
FT /note="K->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:30093673"
FT MUTAGEN 85
FT /note="N->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:30093673"
FT MUTAGEN 136
FT /note="D->A: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:30093673"
FT MUTAGEN 139
FT /note="D->A: Slight decrease in activity."
FT /evidence="ECO:0000269|PubMed:30093673"
FT MUTAGEN 140
FT /note="R->A: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:30093673"
FT MUTAGEN 143
FT /note="E->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:30093673"
FT MUTAGEN 355
FT /note="D->A: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:30093673"
FT STRAND 48..54
FT /evidence="ECO:0007829|PDB:6FQB"
FT HELIX 59..74
FT /evidence="ECO:0007829|PDB:6FQB"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:6FQB"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:6FQB"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:6FQB"
FT HELIX 116..119
FT /evidence="ECO:0007829|PDB:6FQB"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:6FQB"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:6FQB"
FT HELIX 144..156
FT /evidence="ECO:0007829|PDB:6FQB"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:6FQB"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:6FQB"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:6FQB"
FT STRAND 181..186
FT /evidence="ECO:0007829|PDB:6FQB"
FT TURN 206..208
FT /evidence="ECO:0007829|PDB:6FQB"
FT STRAND 213..217
FT /evidence="ECO:0007829|PDB:6FQB"
FT STRAND 223..226
FT /evidence="ECO:0007829|PDB:6FQB"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:6FQB"
FT STRAND 238..247
FT /evidence="ECO:0007829|PDB:6FQB"
FT STRAND 252..256
FT /evidence="ECO:0007829|PDB:6FQB"
FT STRAND 259..265
FT /evidence="ECO:0007829|PDB:6FQB"
FT HELIX 269..283
FT /evidence="ECO:0007829|PDB:6FQB"
FT HELIX 288..298
FT /evidence="ECO:0007829|PDB:6FQB"
FT HELIX 299..302
FT /evidence="ECO:0007829|PDB:6FQB"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:6FQB"
FT STRAND 313..319
FT /evidence="ECO:0007829|PDB:6FQB"
FT HELIX 323..333
FT /evidence="ECO:0007829|PDB:6FQB"
FT STRAND 340..345
FT /evidence="ECO:0007829|PDB:6FQB"
FT TURN 350..352
FT /evidence="ECO:0007829|PDB:6FQB"
FT HELIX 356..360
FT /evidence="ECO:0007829|PDB:6FQB"
FT HELIX 364..369
FT /evidence="ECO:0007829|PDB:6FQB"
FT STRAND 375..379
FT /evidence="ECO:0007829|PDB:6FQB"
FT HELIX 382..391
FT /evidence="ECO:0007829|PDB:6FQB"
FT HELIX 396..398
FT /evidence="ECO:0007829|PDB:6FQB"
FT STRAND 399..401
FT /evidence="ECO:0007829|PDB:6FQB"
FT HELIX 405..413
FT /evidence="ECO:0007829|PDB:6FQB"
FT STRAND 416..424
FT /evidence="ECO:0007829|PDB:6FQB"
FT HELIX 426..432
FT /evidence="ECO:0007829|PDB:6FQB"
SQ SEQUENCE 447 AA; 49576 MW; 7CB20A375AC90754 CRC64;
MNLKTTLGLL AGRSSHFVLS RLGRGSTLPG KVALQFDKDI LQSLAKNYEI VVVTGTNGKT
LTTALTVGIL KEVYGQVLTN PSGANMITGI ATTFLTAKSS KTGKNIAVLE IDEASLSRIC
DYIQPSLFVI TNIFRDQMDR FGEIYTTYNM ILDAIRKVPT ATVLLNGDSP LFYKPTIPNP
IEYFGFDLEK GPAQLAHYNT EGILCPDCQG ILKYEHNTYA NLGAYICEGC GCKRPDLDYR
LTKLVELTNN RSRFVIDGQE YGIQIGGLYN IYNALAAVAI ARFLGADSQL IKQGFDKSRA
VFGRQETFHI GDKECTLVLI KNPVGATQAI EMIKLAPYPF SLSVLLNANY ADGIDTSWIW
DADFEQITDM DIPEINAGGV RHSEIARRLR VTGYPAEKIT ETSNLEQVLK TIENQDCKHA
YILATYTAML EFRELLASRQ IVRKEMN
