ID A0A1M7D463_9FLAO Unreviewed; 768 AA.
AC A0A1M7D463;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=SAMN05444484_102410 {ECO:0000313|EMBL:SHL73979.1};
OS Flavobacterium chilense.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=946677 {ECO:0000313|EMBL:SHL73979.1, ECO:0000313|Proteomes:UP000184028};
RN [1] {ECO:0000313|EMBL:SHL73979.1, ECO:0000313|Proteomes:UP000184028}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24724 {ECO:0000313|EMBL:SHL73979.1,
RC ECO:0000313|Proteomes:UP000184028};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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}.
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DR EMBL; FRBT01000002; SHL73979.1; -; Genomic_DNA.
DR RefSeq; WP_068841879.1; NZ_LSYT01000002.1.
DR AlphaFoldDB; A0A1M7D463; -.
DR STRING; 946677.SAMN05444484_102410; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000184028; 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 Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 71..245
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 428..682
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 768 AA; 86671 MW; 4FD32F479F292094 CRC64;
MATKKNNQSN SNKDINYYKK KFWRVFAYTL LGILAFFLFA SWGLFGSMPS FEDLENPDSN
LATEIISSDG VVIGKYFKTN RSQLKYSDLP KSLVEALVAT EDARFYDHSG IDGRGTLRAV
FSLGTNGGAS TLTQQLAKQL FHGEGSKFLP FRIVQKIKEW IIAIRLERQY TKNEILAMYC
NVYDFGNYSV GVSSAAQTYF SKDPKDLTMD ESAILVGMFK NSGLYNPVRN PEGVKNRRNV
VLSQMEKAKM ITTAEKLRLQ ALPIALKFKL ESHREGTATY FREYLRDYMK KWVTENKKPD
GSDYDIYKDG LKIYTTIDSR MQLHAEEAVS EHMKNLQQQF FIEMKTNKNA PFVNITQAET
DRIMMQAMKN STRWAIMKDM DKSEDDIIAS FKVKTKMRVF TWKGERDTVM TPLDSIRYFK
HFLQSGLMAM EPQTGNIKAW VGGINYKYFQ YDHVGQGARQ VGSTFKPFVY ATAIEQLNMS
PCDSILDGPF MIHKGRHNVT ADWEPRNSDN RYRGMVTLKQ GLANSINTVS AKLIDRTGPE
AVVELTHKLG VKTEIPPQPS IALGAVDITV EDMVAAYSTF ANQGVYVKPQ FLSRIENKSG
EVIYEPIPES HDVLNKDIAF AVIKLLEGVT ETGSGARLRT QGGGSGDNRW TGYPYMFKNP
IAGKTGTTQN QSDGWFMGMV PNLVTGVWVG CEDRSARFKS LTYGQGATAA LPIWGYFMKL
CYADPGLQVS KSEFERPANL SIKVDCYSRP AVVKDTTQTD QNTDEFEL
//
