ID A0A0X8G734_9FLAO Unreviewed; 764 AA.
AC A0A0X8G734;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=Lupro_08355 {ECO:0000313|EMBL:AMC11265.1};
OS Lutibacter profundi.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Lutibacter.
OX NCBI_TaxID=1622118 {ECO:0000313|EMBL:AMC11265.1, ECO:0000313|Proteomes:UP000059672};
RN [1] {ECO:0000313|Proteomes:UP000059672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LP1 {ECO:0000313|Proteomes:UP000059672};
RA Wissuwa J., Le Moine Bauer S., Stokke R., Dahle H., Steen I.H.;
RT "Complete genome sequence of Lutibacter profundus strain LP1.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AMC11265.1, ECO:0000313|Proteomes:UP000059672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LP1 {ECO:0000313|EMBL:AMC11265.1,
RC ECO:0000313|Proteomes:UP000059672};
RX PubMed=27118569; DOI=10.1099/ijsem.0.001105;
RA Le Moine Bauer S., Roalkvam I., Steen I.H., Dahle H.;
RT "Lutibacter profundi sp. nov., isolated from a deep-sea hydrothermal system
RT on the Arctic Mid-Ocean Ridge and emended description of the genus
RT Lutibacter.";
RL Int. J. Syst. Evol. Microbiol. 66:2671-2677(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-
CC Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-
CC (1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-
CC cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-
CC D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl
CC diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+);
CC Xref=Rhea:RHEA:23708, Rhea:RHEA-COMP:9602, Rhea:RHEA-COMP:9603,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58405, ChEBI:CHEBI:60033,
CC ChEBI:CHEBI:78435; EC=2.4.1.129;
CC Evidence={ECO:0000256|ARBA:ARBA00023988};
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DR EMBL; CP013355; AMC11265.1; -; Genomic_DNA.
DR RefSeq; WP_068208645.1; NZ_CP013355.1.
DR AlphaFoldDB; A0A0X8G734; -.
DR STRING; 1622118.Lupro_08355; -.
DR KEGG; lut:Lupro_08355; -.
DR PATRIC; fig|1622118.3.peg.1729; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000059672; Chromosome.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.3810.10; Biosynthetic peptidoglycan transglycosylase-like; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR001264; Glyco_trans_51.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF11; PENICILLIN-BINDING PROTEIN 1B; 1.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
PE 4: Predicted;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000059672}.
FT DOMAIN 66..243
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 428..680
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 745..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..764
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 764 AA; 87397 MW; 03D7A7B24E1165F1 CRC64;
MKKKEMTNNQ FSKYVKWFWF SVLGGVLTLI FLFLLASWGV FGMLPTFEEL ENPEHNLASE
VISIDGKTLG KYFKENRTPV KYKDLPKNLV NALISTEDER FYEHSGIDFK ATFRAILKMG
RDGGGSTITQ QLAKLLFHGE GSKNLPERIL QKVKEYVIAI RLEKQYTKQE ILAMYLNKYD
FLNQAVGIRS ASRIYFGKEP KELTIPESAM LVGMLKNASY FNPLRQSRKK LVKNRRNVVL
HQMFKNHFIS EVQKDSLQKL DLELNVNREG HSDGYATYFR EYLRDFMKKW IKRNPKPDGT
FYNLHRDGLK IYVTIDSRMQ KYAEEAMKEH MSNLQRVFFK EQKHNRTAPF YDLDKKQITN
TIERAMKRSN RWKRMKRSGA SVKEIKASFD KKYEMKVFSW KGDIDTIMSP KDSIRYYKYF
LRSGLLSIEP QSGHIKAWVG GINYKHFQFD AVKQQKRQVG STFKPFVYAT AINQLNLSPC
DKFPNTPYTI PKEKYGMPED WTPVNSGGKY GGELTLKQAL AGSVNVITAK LIDMVNPKNV
VSLAKSAGIE SDILEVPAIA LGSVDLSLYE MVGAYTTFAN KGLRVEPMML QKIEDKNGTV
LEQFIPKSKE VLSEESAYVV INLLEGVTEA GSGVRLRTKW AKYPDNIATG YPYEFTNPIA
GKTGTTQNQS DGWFMGIVPN LATGVWVGGE DRSTHFAGIT KGQGASMALP IWALYYKKLY
ADKSLNISQE EFEKPENLSI DVNCDDTTDV DENLKNTIDE DPEF
//