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Database: UniProt
Entry: A0A0A7LLG5_9BACT
LinkDB: A0A0A7LLG5_9BACT
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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
//
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