ID A0A1D8G374_9ACTN Unreviewed; 915 AA.
AC A0A1D8G374;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN Name=ponA1_3 {ECO:0000313|EMBL:AOT59902.1};
GN ORFNames=A4G23_02760 {ECO:0000313|EMBL:AOT59902.1};
OS Streptomyces rubrolavendulae.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=285473 {ECO:0000313|EMBL:AOT59902.1, ECO:0000313|Proteomes:UP000095349};
RN [1] {ECO:0000313|EMBL:AOT59902.1, ECO:0000313|Proteomes:UP000095349}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MJM4426 {ECO:0000313|EMBL:AOT59902.1,
RC ECO:0000313|Proteomes:UP000095349};
RA Kim J.-G.;
RT "Streptomyces rubrolavendulae MJM4426 Genome sequencing and assembly.";
RL Submitted (SEP-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; CP017316; AOT59902.1; -; Genomic_DNA.
DR RefSeq; WP_069977198.1; NZ_CP017316.1.
DR AlphaFoldDB; A0A1D8G374; -.
DR STRING; 285473.A4G23_02760; -.
DR KEGG; srn:A4G23_02760; -.
DR PATRIC; fig|285473.5.peg.2885; -.
DR OrthoDB; 8865355at2; -.
DR Proteomes; UP000095349; Chromosome.
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:SF34; PENICILLIN-BINDING PROTEIN 1A; 1.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 2.
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:UP000095349};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 128..151
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 172..359
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 465..518
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 557..726
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 696..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 783..915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..831
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 866..906
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 915 AA; 97225 MW; 6F83CB449688D692 CRC64;
MSEHRRKPPQ PQGGGRAAAR RAAQPPGRGP APARDVSTGS PSEPYGEARP YGGRAEARRA
AQRGGRRRVP EGVGAGGAGG RGGGRRGTGG GGRGGRGPGD GHPGKKRLID YPRHDKYGWR
RWVPSWKLVS GLALGFAVLL MGGATLAYSM VGLPNPAKAA TAQNNVYYWS DGTQMAATGG
EVNRQIIAYT EIPQAMQDAV VSAENKTFWT DSGIDPMGIG RALFNMATGG ETQGGSTITQ
QYVKNNRLDN QSQTLDRKFK EMFISIRVNN ELSKKEIMRG YLNTSYFGRG AYGLQAAART
YYGKNAADLS VEECAFLASL LKGSTYYDPA GAPEIDPKAT PQANLDRATK RWNWILDEMV
KDGSLPAAER AGMKFRMPHP PQKQAKLGGQ IGYLVDLAKA YFINNNDQGI TAEDLSKGGY
EIKTTFDKKK VDALAKTVKD VYDKHIDPEK RPDTDTHVEF GGASVNPSTG AIEAIYGGAD
ATKHFTNNAD QTGAQVGSTF KPFVLAAGMT HGVRDRNKGD QQGPEDRTVI DPDTAIYSGK
NKLKIRNYDG SIWRDENNKE WLQVNDDDAD YDNIDLREAM IHSANSPFVQ LGMDIGIPQV
RETAIRAGLL KSSLAQGDVP SFSIGISDPS AIRMAAAYGT FASNGEQRDP YSVTEVKKNG
IAIYKHEDKP TRAFTTAVSS NITDVLVDVV EKGTGKKARL PDRPSAGKTG TTDGNKSAWF
VGYTPQLVTA IDMYRLDDDA SNKDRKFEEM FGTGGREKVH GSSFPSEIWK AYMTEVHKGL
EVKQFPAPEP LDAEPVYGGG AKSPEPSPSS SPSPSPSPST SPSPSPSPSR SKEPEKPGKS
CDPFDWDCEP PTGGTTDGGM TGGADGGGTT GSTDGGTTDG GTTEGGETSP SPGTGGNGNG
NGSGGSGGTP GGWFG
//
