ID A0A098LBF7_9BACT Unreviewed; 763 AA.
AC A0A098LBF7;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=MYP_940 {ECO:0000313|EMBL:GAL83713.1};
OS Sporocytophaga myxococcoides.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae;
OC Sporocytophaga.
OX NCBI_TaxID=153721 {ECO:0000313|EMBL:GAL83713.1, ECO:0000313|Proteomes:UP000030185};
RN [1] {ECO:0000313|EMBL:GAL83713.1, ECO:0000313|Proteomes:UP000030185}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG-01 {ECO:0000313|EMBL:GAL83713.1,
RC ECO:0000313|Proteomes:UP000030185};
RA Liu L., Gao P.J., Chen G.J., Wang L.S.;
RT "Sporocytophaga myxococcoides PG-01 genome sequencing.";
RL Submitted (SEP-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=2.4.1.129;
CC Evidence={ECO:0000256|ARBA:ARBA00023988};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAL83713.1}.
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DR EMBL; BBLT01000002; GAL83713.1; -; Genomic_DNA.
DR RefSeq; WP_045459354.1; NZ_BBLT01000002.1.
DR AlphaFoldDB; A0A098LBF7; -.
DR STRING; 153721.MYP_940; -.
DR eggNOG; COG5009; Bacteria.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000030185; Unassembled WGS sequence.
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; 2.
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:SF11; PENICILLIN-BINDING PROTEIN 1B; 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:UP000030185};
KW Transferase {ECO:0000313|EMBL:GAL83713.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 70..253
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 428..673
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 744..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 763 AA; 85767 MW; 824A8989B3458424 CRC64;
MSKSNFFISA FIKSIWIGFI VGIGSLVLYV YFVSINFLGL FGPMPSLEAL ENPKSEVASE
LYTADNVLLG KYFKENRTPV DFEKLSPNLV NALTATEDSR FEEHSGIDLR GMGRVFFKTI
ILGQRNSGGG STLSQQLAKN LFQTRSALYK GKLSKGTLGK VIFKTKEWIT AVKIERAYTK
KEIMTMYLNT VDFGSNSFGI EVASKTFFNT TPDSLKIEEA AVLVGLLKAP TTYSPVFNPD
SSTSRRNTVI SQMAKYGYLT SIKADSIKKL PIALDYNVEN HNKGSATYFR SLITSYLIPW
CRERGLDLYS DGLKIYTTLD SKMQKYAEES VASHMKEEQR KFFEHWKGKS PWTDEQGKVI
PNFIETAAKR SDRYRALKLQ YGNDTVKIMK VMKTPIKMKI FSWDGEIDTL MSPIDSIKYY
KHFLHCGFMA MDPHSGYIKA WVGGIDHKHF KYDHVKQGKR QPGSTFKPFV YASAIDLGYS
PCYELPDLPV TFPTADVNKT WTPQNSNGEG FTGEMFTLRK AMANSINSIT ANLMKEIGPQ
VVVNNAKRMG ITSPLDPVPA LCLGVSDVSI YELVGAYGTF VNNGFWTEPF FITKIEDKNG
NVLQEFIPKS VEVFDEETAY LMVHMLKGAT EEKGGTALGL NKYGLLWNGY EIGGKTGTTQ
NYSDGWFMGI TPKLVAGAWV GGDDRCIHFR SMDLGQGARM AMPLWAIFMK KVFADSTLGL
IKERFPRPSK LSVEIDCKRY KEKSSQHSDS LQQKHQQVLP IEF
//
