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Database: UniProt
Entry: A0A0X8G734_9FLAO
LinkDB: A0A0X8G734_9FLAO
Original site: A0A0X8G734_9FLAO 
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
//
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