ID C7R038_JONDD Unreviewed; 784 AA.
AC C7R038;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN OrderedLocusNames=Jden_0432 {ECO:0000313|EMBL:ACV08097.1};
OS Jonesia denitrificans (strain ATCC 14870 / DSM 20603 / BCRC 15368 / CIP
OS 55.134 / JCM 11481 / NBRC 15587 / NCTC 10816 / Prevot 55134) (Listeria
OS denitrificans).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Jonesiaceae;
OC Jonesia.
OX NCBI_TaxID=471856 {ECO:0000313|EMBL:ACV08097.1, ECO:0000313|Proteomes:UP000000628};
RN [1] {ECO:0000313|EMBL:ACV08097.1, ECO:0000313|Proteomes:UP000000628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14870 / DSM 20603 / BCRC 15368 / CIP 55.134 / JCM 11481 /
RC NBRC 15587 / NCTC 10816 / Prevot 55134
RC {ECO:0000313|Proteomes:UP000000628};
RX PubMed=21304666; DOI=10.4056/sigs.41646;
RA Pukall R., Gehrich-Schroter G., Lapidus A., Nolan M., Glavina Del Rio T.,
RA Lucas S., Chen F., Tice H., Pitluck S., Cheng J.F., Copeland A.,
RA Saunders E., Brettin T., Detter J.C., Bruce D., Goodwin L., Pati A.,
RA Ivanova N., Mavromatis K., Ovchinnikova G., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Goker M.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P., Han C.;
RT "Complete genome sequence of Jonesia denitrificans type strain (Prevot
RT 55134).";
RL Stand. Genomic Sci. 1:262-269(2009).
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; CP001706; ACV08097.1; -; Genomic_DNA.
DR AlphaFoldDB; C7R038; -.
DR STRING; 471856.Jden_0432; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR KEGG; jde:Jden_0432; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_2_6_11; -.
DR Proteomes; UP000000628; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000000628};
KW Transferase {ECO:0000313|EMBL:ACV08097.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 39..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 105..289
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 395..668
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 720..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..778
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 784 AA; 83669 MW; 4D0535B263EFF287 CRC64;
MPNPARDDLP HGPSSSVSDS PGLLSSSTAR RAPVNPFQVA GLIIVFLALS VIGGVLAAGL
VVPFAAGAST AASTATETFY DLPTELEIDE PSQASKIYAR DGKTLLATYY SEYRLIVPLD
EISEHMQNAV VATEDQRFWS HGGVDVRGIM RAASENIQGN MQGGSTLTQQ YVKNVLIHKA
SKEGDILAVE EARESTLERK LREAKLAINL EKSMPKEEIL ENYLNLAQFG SKVYGVETAA
NYYFNKSAKD LNIVESATIA GVTQRPSSWD PSMNPDDAQR RRNIVLSLMY QQGYITREEH
DEAVATPLEE TLDLQELHNG CEGAGYNGFF CDYVTKSIIN DPAFGETEDE RTEKLYRGGL
TIVTTLDPKK QRYAYRAVRD GVPRDNAKGF ASAITSVEPG TGEIVAMAQN RRYVPNATKS
KTATSVNYSA GSSMGGSNGF QVGSTFKAFT LAEWFKEGHT LRESVNATRK RWVSNQFKAS
CVALGTEPWH PNNVDGLATG NISVEKATAW SVNTAFASIL SKLDLCKVAD TAYDIGFRPS
HPSADGKVKT VPSMTLGIQE SSPLDMASAY ATFASGGVYC EPRALLKVTD TNGEELPIKG
KNCRQTLNKD VANAMNYALG KVIQPGGGAS ASALSGGRPA AGKTGTSNDN SNAWFIGYTP
QLSTAVWMGH PDNQTIRMIG VNIAGRNYPR VYGSTIPAPI WKTYMDQALA KESKEGFDPI
PASLLGSYPK PTPPPSTGNS GSSNKPDSGS SGGNTRNGGS NNGGGNNGGS SNNGGDRGNS
GGDD
//
