GenomeNet

Database: UniProt
Entry: F5VS46_STROR
LinkDB: F5VS46_STROR
Original site: F5VS46_STROR 
ID   F5VS46_STROR            Unreviewed;       447 AA.
AC   F5VS46;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   24-JAN-2024, entry version 39.
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=HMPREF9968_1395 {ECO:0000313|EMBL:EGL92467.1};
OS   Streptococcus oralis SK255.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1005704 {ECO:0000313|EMBL:EGL92467.1, ECO:0000313|Proteomes:UP000003695};
RN   [1] {ECO:0000313|EMBL:EGL92467.1, ECO:0000313|Proteomes:UP000003695}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK255 {ECO:0000313|EMBL:EGL92467.1,
RC   ECO:0000313|Proteomes:UP000003695};
RA   Durkin A.S., Radune D., Hostetler J., Torralba M., Gillis M., Methe B.,
RA   Sutton G., Nelson K.E.;
RL   Submitted (APR-2011) 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|ARBA:ARBA00004752, 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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGL92467.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AFNM01000006; EGL92467.1; -; Genomic_DNA.
DR   AlphaFoldDB; F5VS46; -.
DR   PATRIC; fig|1005704.3.peg.67; -.
DR   eggNOG; COG0770; Bacteria.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000003695; Unassembled WGS sequence.
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   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|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_02214}; Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_02214};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_02214}.
FT   DOMAIN          53..190
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          319..429
FT                   /note="Lipid II isoglutaminyl synthase (glutamine-
FT                   hydrolyzing) subunit MurT C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08353"
FT   ACT_SITE        355
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02214"
FT   BINDING         205
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02214"
FT   BINDING         208
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02214"
FT   BINDING         227
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02214"
FT   BINDING         230
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02214"
SQ   SEQUENCE   447 AA;  49730 MW;  F955BDC68FEEDB03 CRC64;
     MKLKTTLGLL AGRSSHFILS RLGRGSTLPG KLALQFDKDI LQNLAKNYEI VVVTGTNGKT
     LTTALTVGIL KEVYGQVLTN PSGANMITGI TTTFLTAKSS KTGKNIAVLE IDEASLSRIC
     DYIHPSLFVI TNIFRDQMDR YGEIYTTYNM ILDAIRKVPT ATVLLNGDSP LFYKPAIPNP
     VQYFGFDLEK GPAQLAHYNT EGILCPDCQG ILKYELNTYA NLGAYICENC GCKRPNLDYR
     LTKLVELTNN RSRFVIDGQE YGIQIGGLYN IYNALAAVAI ARFLGADSQR IKQGFDKSRA
     VFGRQETFHI GDKECTLVLI KNPVGATQAI EMIKLAPYPF SLSVLLNANY ADGIDTSWIW
     DADFEQITDM DIPEINAGGV RHSEIARRLR VTGYPAEKIT ETSNLEQVLK TIENQDCKHA
     YILATYTAML EFRELLASRQ IVRKEMN
//
DBGET integrated database retrieval system