ID   M4RDR2_9BIFI            Unreviewed;       708 AA.
AC   M4RDR2;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=D805_0431 {ECO:0000313|EMBL:AGH40698.1};
OS   Bifidobacterium thermophilum RBL67.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=1254439 {ECO:0000313|EMBL:AGH40698.1, ECO:0000313|Proteomes:UP000011835};
RN   [1] {ECO:0000313|EMBL:AGH40698.1, ECO:0000313|Proteomes:UP000011835}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RBL67 {ECO:0000313|EMBL:AGH40698.1,
RC   ECO:0000313|Proteomes:UP000011835};
RX   PubMed=23640377;
RA   Jans C., Lacroix C., Follador R., Stevens M.J.;
RT   "Complete Genome Sequence of the Probiotic Bifidobacterium thermophilum
RT   Strain RBL67.";
RL   Genome Announc. 1:E00191-13(2013).
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; CP004346; AGH40698.1; -; Genomic_DNA.
DR   AlphaFoldDB; M4RDR2; -.
DR   KEGG; btp:D805_0431; -.
DR   PATRIC; fig|1254439.12.peg.432; -.
DR   eggNOG; COG0744; Bacteria.
DR   HOGENOM; CLU_006354_2_6_11; -.
DR   Proteomes; UP000011835; 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:SF33; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; 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}.
FT   DOMAIN          77..267
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          371..648
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   708 AA;  76341 MW;  ADC65A6A83BDDD36 CRC64;
     MPKKNSLTAR RALALLLAYL TLCIAGGVVV SLMAMPAVFG ANNAAKALAP SLTVEGIDFD
     VTSLPQKSTL YASDGKTVIA SFYAQNREVV PIKNISVYMQ RAVVAREDRR FFEHAGVDVQ
     GVLRAFVQTY VAKGDTQGGS SLTQQYVKNV LMVKAREDDD PIAEYHASED TVARKLREML
     IAVQMEKKYS KYEILQGYLN IAQFGSGSLY GVEAAAKRYF NTTAANLSVV QAATIAAITK
     NPEKYDPSIE ANQKTSEEQR NIVLDLMLQE KFITKAQHDK AKATPLKDTL NIQSVQQGCQ
     VAGDAAFFCS YVTNQILNSK EFGNTAQARQ KLLNEGGLEI YTTMDVNANN AAMKAARDTI
     PVDDPTGFEV TIAAVKPGTG EVLGFGINRI YDATDAAKTD PTRTSINYAV DQKDGGGIGF
     NVGSTWKPIN MIAWMLQGHS INESLRTYTS YANSSFNCSK FSGHGTWSLH NSEGGTVSRE
     TPLQGLIKSH NTTQASMTQQ IGLCAIADAA KTVGYHNAIL GQEDVYSANS FNPPMIIGSV
     QASPLTMANV YATIAANGVE CTPIAIKKVI KQNGKSVKVP SANCHQAIAP EIAQTTAYAL
     NQGVLKGEAK AAQLDNNRKT FAKTGTNEQT YMLTAGFVPN QVAAFVAVGN AEVQESFSGK
     TINGVSHGTW YGMYIASPAW KEFVDTYLAA INAPIDSDYG TPAEQYMR
//