ID H8L136_FRAAD Unreviewed; 795 AA.
AC H8L136;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 18-JUN-2025, entry version 68.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00044770};
DE EC=2.4.99.28 {ECO:0000256|ARBA:ARBA00044770};
GN OrderedLocusNames=Fraau_2857 {ECO:0000313|EMBL:AFC87191.1};
OS Frateuria aurantia (strain ATCC 33424 / DSM 6220 / KCTC 2777 / LMG 1558 /
OS NBRC 3245 / NCIMB 13370) (Acetobacter aurantius).
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Lysobacterales; Rhodanobacteraceae; Frateuria.
OX NCBI_TaxID=767434 {ECO:0000313|EMBL:AFC87191.1, ECO:0000313|Proteomes:UP000005234};
RN [1] {ECO:0000313|Proteomes:UP000005234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33424 / DSM 6220 / KCTC 2777 / LMG 1558 / NBRC 3245 /
RC NCIMB 13370 {ECO:0000313|Proteomes:UP000005234};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Teshima H.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Frateuria aurantia DSM 6220.";
RL Submitted (FEB-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=2.4.99.28;
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; CP003350; AFC87191.1; -; Genomic_DNA.
DR AlphaFoldDB; H8L136; -.
DR STRING; 767434.Fraau_2857; -.
DR KEGG; fau:Fraau_2857; -.
DR eggNOG; COG4953; Bacteria.
DR HOGENOM; CLU_006354_7_3_6; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000005234; 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:UniProtKB-UniPathway.
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:UP000005234};
KW Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT DOMAIN 76..243
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 320..546
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 704..788
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 795 AA; 84994 MW; A7B6FBECA6342AEA CRC64;
MSPAGGPEVV GAARASSRCR RGRRIGGSLL AGVLSALLLC RVLDLLFPLP LPAPDGGSTV
VLARDGTPLR AFADARGVWS YPATVDQVSP LYRQALLNYE DRWFYRHPGI NPLALLRGLA
GLLRDGHIHS GGSTLTMQVA RIISPIPHSV GGKLVQIFRA LQLEVHLDKT QILQLYLDHA
PFGGPIEGVE AASWAYLGKP ASQLSHAEAA LLAVLPQSPS RFRPDRHPER ARQARDKVLQ
RMQAQGVWTA AQVRDARLEP VVARSLHTPI HAALLAQRLH AAQPRQRRIV TTLDADLQQA
VEERVGEVVA RLPPRTSAAV LVIDNASLQA RVYVGSAAFG DARRLGDVDM VRAPRSPGST
LKPFLYGLAL DDGLITSQSL LVDAPQDFGG YRPGNFDESF HGPVSVAEAL QRSLNVPAVQ
VLDQLGANRF VARLANGGLD LQWPAGASPN LSVILGGASA RLEQLVGAYS ALNHEGIAGL
PRYTLQQPLR QGRLLSPGAA WIIRDILGHN PAQVEGAPLA DTIDSRSDIA WKTGTSYGYR
DAWAIGVSDA WTFGVWIGRP DGSPSPGQYG AATALPLMFD ITRMLPPGRG TSHDARPASV
RSVDICWPLG GAAAATPAAL CRRRRTAWVL DDALPPTFAE HDAGAWIGGR LRLRLDANGR
RLSATCHGRG EHEAVIARWP TLLAPWLSLA EALPPLAPGC PADSLQAASP IRIAGLDDQA
VLRRAPNSQT PLAVTLQALG AEGDVQWLLD GRLQGQTRNE TSIRIALPEV GKHQITALGQ
GGSFARIEVA VQSMN
//
