ID A0A1R1QN37_9BACI Unreviewed; 712 AA.
AC A0A1R1QN37; A0A1R1RW81;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=BTA30_12765 {ECO:0000313|EMBL:OMI30229.1}, BW143_09105
GN {ECO:0000313|EMBL:OMI06085.1};
OS Bacillus swezeyi.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1925020 {ECO:0000313|EMBL:OMI06085.1, ECO:0000313|Proteomes:UP000187367};
RN [1] {ECO:0000313|EMBL:OMI06085.1, ECO:0000313|Proteomes:UP000187367}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-41282 {ECO:0000313|EMBL:OMI06085.1,
RC ECO:0000313|Proteomes:UP000187367}, and NRRL B-41294
RC {ECO:0000313|EMBL:OMI30229.1, ECO:0000313|Proteomes:UP000187536};
RA Dunlap C.;
RT "Bacillus phylogenomics.";
RL Submitted (JAN-2017) 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:OMI06085.1}.
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DR EMBL; MTJL01000016; OMI06085.1; -; Genomic_DNA.
DR EMBL; MRBK01000013; OMI30229.1; -; Genomic_DNA.
DR RefSeq; WP_076761696.1; NZ_MTJL01000016.1.
DR AlphaFoldDB; A0A1R1QN37; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000187367; Unassembled WGS sequence.
DR Proteomes; UP000187536; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; 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:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase 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 NCBIfam; TIGR02074; PBP_1a_fam; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF36; PENICILLIN-BINDING PROTEIN 1F; 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 5..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 52..226
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 318..591
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 712 AA; 79279 MW; 657DEBE64589C7DE CRC64;
MRKRFFIPII ITAAIFLLSL IGYITILFLG DYVIDEKKLI FHASSKIVDQ NGEEVASLYT
ENRSPVSIGE VPDEVKHAFI AVEDKRFYEH HGIDFKSVSR AIYKDILAGG KVEGGSTITQ
QLAKNTFLTN DKTFLRKTKE VIIAINLERD YSKDKLLEMY LNQLYFGHGV YGIQAAANYY
FNKDAKDLNV SEGAVLASIP KAPSTYSPIL NPEKSRERRN VVLSMMNEQG YISSRETVRA
QGSTLGLHVK EKSKNPWIDS YIDLVIKEAE DRYSISSEQL LQGGYTISVP LDVSIQKAAY
TLMKEDAYFP GTDQKAEGSA VFIDNKTGGV VAALGGRDYL PKSYNRATAA RQPGSTFKPL
AVYGPALEEK LFKPYSLLED KQLSYGGYAP KNYDGQYEGK VSMVDALTDS KNAPAVWTLN
EIGIETAKPY VSRLGMNIPD EGLALALGGL EEGVSPLQLA GAYRTFANSG KYDKPYFIRK
ITDESGNVLY RHEDKPEKVF SKQTAWNMTR MLQEVVKSGT GKAGEFSGEI AGKTGSTTFT
GKEGGTKDAW FAGYTPGVTG AVWMGYDKTD EAHYLKGGSS YPTRLFKDIL KRSKQKTDTF
KKPEGVKDLD RPIHLEDLES AEADYSFTPM GLITVSLKWH EQEDKRAEYR IYEKKNGKEA
LIKTVTGKGS YEIPYANIFS DVSYRIVPYN PQTKTEGKGT DFIKPKIFPS GH
//
