ID A0A0J0UZD4_9ACTN Unreviewed; 722 AA.
AC A0A0J0UZD4;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=IMCC26207_105215 {ECO:0000313|EMBL:KLR62139.1};
OS Actinobacteria bacterium IMCC26207.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1641811 {ECO:0000313|EMBL:KLR62139.1, ECO:0000313|Proteomes:UP000036180};
RN [1] {ECO:0000313|EMBL:KLR62139.1, ECO:0000313|Proteomes:UP000036180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC26207 {ECO:0000313|EMBL:KLR62139.1,
RC ECO:0000313|Proteomes:UP000036180};
RA Kim S., Cho J.-C.;
RT "Genome sequence of freshwater Actinobacteria.";
RL Submitted (MAY-2015) 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 -!- 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:KLR62139.1}.
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DR EMBL; LCZK01000005; KLR62139.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J0UZD4; -.
DR STRING; 1641811.IMCC26207_105215; -.
DR PATRIC; fig|1641811.3.peg.807; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000036180; 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; 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 ECO:0000313|EMBL:KLR62139.1};
KW Glycosyltransferase {ECO:0000313|EMBL:KLR62139.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KLR62139.1};
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:UP000036180};
KW Transferase {ECO:0000313|EMBL:KLR62139.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 68..247
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 348..616
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 658..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..699
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..722
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 722 AA; 75660 MW; EF044111378FCD39 CRC64;
MSRPLSLLLR FTAITLVGAC VFALIASFLI PEMANMSGGG SYNEGTEIAL PDLLQGSVIT
DMNGKPSGSL VGSENRVIIP LSQVSTQMQQ AVLAVEDSDF YVHHGVSAKS VLRAVRANSA
AGGVAQGGST ITQQLVKLSL VGNEQSMKRK VKEASLALQL EQQFCKDRPR RDCKDEILER
YLNTVYLGRG AYGVEAAAQM YFGKSAAELD WGDAAVLASL IRNPTGYDPI RFPEVAARRR
QVVLGRMAEV GAITAQEAAL IEETPLPTEI VKGSSSATAQ DLTYFERKVR DELLRAEWLA
PTEALRRERI FNGGLMITST LDPRAQMLAE AASASNPIKK ANPETVAAVA VVEPSSGSVR
AVVGQTDLPG QGLVEIATPQ VGRSPGSSFK AFTLLAALEA GYSIRDSILA APAPQKLYKG
WGIKDSTWPS GCKGGTIELA KATSSSNNCA FARLQAAVGG EKVVDVARRL GIDTLTDESA
EYPSLTLGGT TVRPLEMAAA YAAIANDGIY NPAHFITKVT DQAGAVLFEY VPATEQAISV
DVAQQATVAL QGVVTGGTYK GGSLPNRQPA AGKTGTNEAA GGENTDVWFV GFTPQIATAV
WIGNPAGQTE MKGGRVQGGT VAGKVWHTFM APYLEGTTVQ QFATPGRIKT SRKVIPDPWT
KAMSSAEKAG TTSTTKTTIA GSSTSKPPGS STPAATTAPT TAAPAPDPEP VPTPEPPPEP
AP
//
