ID A0A1I6J8A8_9MICO Unreviewed; 804 AA.
AC A0A1I6J8A8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=SAMN05428970_1869 {ECO:0000313|EMBL:SFR75182.1};
OS Agromyces sp. CF514.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Agromyces.
OX NCBI_TaxID=1881031 {ECO:0000313|EMBL:SFR75182.1, ECO:0000313|Proteomes:UP000199174};
RN [1] {ECO:0000313|EMBL:SFR75182.1, ECO:0000313|Proteomes:UP000199174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF514 {ECO:0000313|EMBL:SFR75182.1,
RC ECO:0000313|Proteomes:UP000199174};
RA de Groot N.N.;
RL Submitted (OCT-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};
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DR EMBL; FOZD01000001; SFR75182.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6J8A8; -.
DR STRING; 1881031.SAMN05428970_1869; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000199174; 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; 2.
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:SFR75182.1}; 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 20..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 90..163
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 206..312
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 419..712
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 741..804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 756..776
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..804
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 804 AA; 85150 MW; 3EB6E0CEEF73F20B CRC64;
MTERNKRNRD FAETRTPLGV LGGLVGIVVA STAAAALIVV GVTPALATVG MAASGTIDTF
ERLPGYLQIG ELSQKSNIYA TRPDGSPLLL ASFYDQNRVE VEWDQISPFV KDATIAGEDP
RFYDHGGVDL QGTIRAALTT AAGRDTQGGS SIAQQYVKNV RVQQCEREAD VTAFEDMAED
EVAALTGDER FALIEEERLS CYDSATETSI DRKLKEMRLA IGVEKRYSKN DILLGYLNIA
GFGGTVYGIE AAANYYFSTS AANLTLPQAA SLVAIVNNPV KFQLDKPDSE TNGAANGYAA
NRDRRDYLLR QMLHEKKITQ AQYDEAIATP VEPKITEPST GCQTAGGSAY FCDYVKHILQ
NDPTFGDDDE TRMLNFRRGG YQVYTSLDLD LQAAAERAIA ENVPSTYPGW DLGGVISSVE
VGTGRVLAMA QNKQYSQDPA VVNGNPNFTG INYNTDYDYG GSSGFQPGSS YKVFTLAEWL
AEGHALTERV NSSRKSNWGA FNDSCLGTQY ADPGWNPRND ANEPGGNYSA LESTIGSINT
GFLGMAKLID QCGIASKAEA FGVHRADGNP LVHFPSAVLG INEVAPLSMA VAFAGIANDG
VACTPVAIDR IVGADGEDIT PPKSTCAAAV TPEVAGAMHY AMSRVMSSGT GQQSSNATSP
WVPLIGKTGT TDGAKDTWMV GASTEVATAV AVVSVNGDAN QRGISFDSGS AATARHRMWP
IVMSAASAKY GGGAFRMDGP GPVAPFTSPT PFDDVPKYVE PTPTPPPAPA PAPAPSPQTQ
TQGGVGDRTL EPRDDEGRGG GRGR
//
