ID A0A0S7BZA8_9BACT Unreviewed; 784 AA.
AC A0A0S7BZA8;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=TBC1_11455 {ECO:0000313|EMBL:GAP42326.1};
OS Lentimicrobium saccharophilum.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Lentimicrobiaceae;
OC Lentimicrobium.
OX NCBI_TaxID=1678841 {ECO:0000313|EMBL:GAP42326.1};
RN [1] {ECO:0000313|EMBL:GAP42326.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TBC1 {ECO:0000313|EMBL:GAP42326.1};
RA Tourlousse D.M., Matsuura N., Sun L., Toyonaga M., Kuroda K., Ohashi A.,
RA Cruz R., Yamaguchi T., Sekiguchi Y.;
RT "Draft Genome Sequence of Bacteroidales Strain TBC1, a Novel Isolate from a
RT Methanogenic Wastewater Treatment System.";
RL Genome Announc. 3:e01168-15(2015).
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; DF968182; GAP42326.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S7BZA8; -.
DR STRING; 1678841.TBC1_11455; -.
DR PATRIC; fig|1678841.3.peg.522; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000053091; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 2.
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 ECO:0000313|EMBL:GAP42326.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000053091};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 69..246
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 463..700
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 784 AA; 89235 MW; 51198426A14A18A8 CRC64;
MSKKPKGSTA DVNSWKKRFW KAYLVVFVFI VLLFTAISSG LLGFMPSFEE LENPKSNLAS
EIISADQELL GKYYIENRSN INYKDLSPNL VNAIIATEDA RFEKHSGVDV KALFRVTFGL
LTGSNKGGGS TLSQQLAKNL FPRKANRNFF ETVFIKLKEW VTAIKLERNY TKEEILAMYF
NTVDFGSNSF GIKSAAKTFF NKLPSELTIE ESAMLVGMLK APTFFSPVRN PERAIKRREV
VLHQMERYGY ISEHAYDSIR VIPLDMSKYR QQDHTSGTAT YFREYLRMAM SAKKPHRKNY
IDKQAYTEDS LQWVSNPIYG WIEKNPKPDG SKYNLYKDGL RIYTTINSRM QRYAEEAVAE
HMGGDIQPAF FRHWKGREEA PFDFPKSQVK AEAHKLLNAS MKRSERYRKM KAAGLPEDSI
RLAFHTKTPM KVFTWQGERD TIMTPWDSIR YCKFFLQAGL LSVEPQTGFV RAYVGGINYS
HFQFDHVKMA RRQVGSTFKP FVYTLAMQEG DFSPCTKVAN IQYSIDLPEG GRWEPRNSND
YKKGEMVTLK EALANSINWI SAFLIKRYSP MAVIKIARKM GVVSPIDPVP SISLGTPDLT
LYEMTGAMNT FAAKGVYIEP LFVTRIEDKN GNVLARFMPR QEEAMSEETA FLMLELMKGV
VESGTGVRLR YKYGIANPVA GKTGTTQNNS DGWFMGLTPD LVTGVWVGGE DRSIRFRTIT
LGQGANMALP IWALYMKRIY ADPKLKLSQG DFEGPSGPLS VEIDCKKYEE LQKQQKSKYS
PGDF
//