ID A0A0A7LLG5_9BACT Unreviewed; 753 AA.
AC A0A0A7LLG5;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 18-JUN-2025, entry version 39.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00044770};
DE EC=2.4.99.28 {ECO:0000256|ARBA:ARBA00044770};
GN ORFNames=PK28_05260 {ECO:0000313|EMBL:AIZ63243.1};
OS Hymenobacter sp. DG25B.
OC Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
OC Hymenobacteraceae; Hymenobacter.
OX NCBI_TaxID=1385664 {ECO:0000313|EMBL:AIZ63243.1, ECO:0000313|Proteomes:UP000030789};
RN [1] {ECO:0000313|EMBL:AIZ63243.1, ECO:0000313|Proteomes:UP000030789}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG25B {ECO:0000313|EMBL:AIZ63243.1,
RC ECO:0000313|Proteomes:UP000030789};
RA Jung H.-Y., Kim M.K., Srinivasan S., Lim S.;
RT "Hymenobacter radioresistens genome sequence.";
RL Submitted (NOV-2014) 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=2.4.99.28;
CC Evidence={ECO:0000256|ARBA:ARBA00049902};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the transpeptidase
CC family. {ECO:0000256|ARBA:ARBA00007090}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC glycosyltransferase 51 family. {ECO:0000256|ARBA:ARBA00007739}.
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DR EMBL; CP010054; AIZ63243.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A7LLG5; -.
DR STRING; 1385664.PK28_05260; -.
DR KEGG; hyd:PK28_05260; -.
DR HOGENOM; CLU_006354_7_3_10; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000030789; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:TreeGrafter.
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:InterPro.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:InterPro.
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; IPR050396; Glycosyltr_51/Transpeptidase.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR011815; PBP_1c.
DR InterPro; IPR009647; PBP_C.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR NCBIfam; TIGR02073; PBP_1c; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF15; PENICILLIN-BINDING PROTEIN 1C; 1.
DR Pfam; PF06832; BiPBP_C; 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 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022670};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000030789};
KW Transferase {ECO:0000313|EMBL:AIZ63243.1}.
FT DOMAIN 33..206
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 286..524
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 664..746
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 753 AA; 83888 MW; C71AE62129A43089 CRC64;
MLVVGGGFLL NWFFPIPPPP QYSPIVLAAD GSVLHAYLNP TQKWRMKTEL REITPALRKA
IVEKEDRWFY WHLGVNPVAL VQAAARNIFG TGRTTGASTI TMQVARLLEP KERSFGNKLL
EMLRATQLEL HYSKAEILQL YLNLVPYGGN VEGVKSAALL YFQQPPDYLS LAQTVTLAII
PNRPRGLILG KNNAAVLQER NRWLRRFAQA GLFPQQDIED ALLEPLQVRR HAAPALAPHF
SRRLVRQFPQ QAIIRSALSR NKQSKVEDLT RNYVRRLYER GITQAAVLVI NNRTRQVEAY
VGSADFRDFA HQGQNDGVQA VRSPGSTLKP FLYALAMDRG LVTPKRMLPD VPTNFQGYRP
ENYDKHCNGE VTLERALAYS LNIPAVRVLQ ELGVPSFTDK LRQAGFRNIT RNAPRLGLSS
ILGGCGASLE ELTNLYVTLA NGGRYSHLRL TASPKTSSNR LFSEASAFLT TDILAQLTRP
DLPLGAASSL RLPKVAWKTG TSYGRRDAWS IGYNKQYTIG VWVGNFNGQG SPALTGADVA
TPLLFDLFNA VAYNSPNDWF VPPAALDFRL VCAETGLVPG ENCPNQLIDY FLPGVSSGQR
CQHQREVLLS ADGHFTYCRA CAPAAGFRRE LYPNLLPEIA AYKEAQGIPY RRLPEHNPQC
QLVQAGPERA PSITSPTPNT EYVLNSHEKQ QLLLSCTTDN EVRQVYWYVN DQFLRAAGAN
ERVFFRPPTG PVKISCADDH GRNTDVLVTV TQL
//