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Database: UniProt
Entry: R6FBN8_9BACE
LinkDB: R6FBN8_9BACE
Original site: R6FBN8_9BACE 
ID   R6FBN8_9BACE            Unreviewed;       775 AA.
AC   R6FBN8;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-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=BN744_01787 {ECO:0000313|EMBL:CDB10518.1};
OS   Bacteroides sp. CAG:633.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=1262744 {ECO:0000313|EMBL:CDB10518.1, ECO:0000313|Proteomes:UP000018121};
RN   [1] {ECO:0000313|EMBL:CDB10518.1, ECO:0000313|Proteomes:UP000018121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:633 {ECO:0000313|Proteomes:UP000018121};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752}.
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:CDB10518.1}.
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DR   EMBL; CBDA010000143; CDB10518.1; -; Genomic_DNA.
DR   RefSeq; WP_022163289.1; NZ_FR883088.1.
DR   AlphaFoldDB; R6FBN8; -.
DR   Proteomes; UP000018121; Unassembled WGS sequence.
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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000018121}.
FT   DOMAIN          58..238
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          451..690
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          747..775
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   775 AA;  88611 MW;  E368F00FCC8234E0 CRC64;
     MIRKIVKILW ILLALGIMAC AAVFFAIAKG WIGYMPPVED LENPNYKFAT EVLSEDGVVL
     GTYSYSKENR VYVGYQDLSP HIINALIATE DVRFAEHSGI DAKALFRAIL KRGVLMQKNA
     GGGSTITQQL SKQLYSPSAD NVMERLFQKP IEWVIAVKLE RYYTKEEILT MYLNKFDFLN
     NAVGVKTAAY TYFGCEPKNL KIEEAATLVG MCKNPSLYNP VRYNERTRGR RNVVLDQMRK
     AGYITQEECD SLQALPLKLT YHRVDHNEGL ATYFREYLRG VLNAKKPVRS EYRGWQMQKY
     YEDSLDWENN PLFGWCEKNR KKDGSKYNLY TDGLKIYTTI DSRMQKYAEE AVTEHLKELQ
     YYFFKEKKGQ KTAPYTRELT QEQVNSILDR AMKQSDRYRK MKEGGASEKE IRKAFDTPEE
     MTVFTWNGER DTVMTPMDSI RYYKFFLRAG FMSMDPRNGH VKAYVGGPNH HYFKYDMGMV
     GRRQIGSTMK PYVYALAMEN GFSPCDQMRH VEFHGFDENG TPWSPRNANN KRYGEMVTLK
     WGLANSDNWI TANLMSKLNP YELKRLVHSF GVRNREIVPS IALCLGPCEI SVGEMVSAYT
     AFPNRGIRVA PLFVTRIEDN EGNVLATFAP EMQEVISVSS AYKMLVMLRA VINEGTGGRV
     RRLGVKADMG GKTGTTNNNS DGWFMGFTPS LVSGCWVGGE DRDIHFDRMF YGQGASMALP
     IWAKYMVKVY ADKTLGYDET ETFQLPEGYD PCKDSEATDS TVTDEPIQGL DDLFN
//
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