ID A0A1E7L2Q3_9ACTN Unreviewed; 818 AA.
AC A0A1E7L2Q3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
DE Flags: Fragment;
GN ORFNames=AN218_17350 {ECO:0000313|EMBL:OEV10459.1};
OS Streptomyces nanshensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=518642 {ECO:0000313|EMBL:OEV10459.1, ECO:0000313|Proteomes:UP000176005};
RN [1] {ECO:0000313|EMBL:OEV10459.1, ECO:0000313|Proteomes:UP000176005}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCSIO 10429 {ECO:0000313|EMBL:OEV10459.1,
RC ECO:0000313|Proteomes:UP000176005};
RX PubMed=27446038; DOI=10.3389/fmicb.2016.00998;
RA Tian X., Zhang Z., Yang T., Chen M., Li J., Chen F., Yang J., Li W.,
RA Zhang B., Zhang Z., Wu J., Zhang C., Long L., Xiao J.;
RT "Comparative Genomics Analysis of Streptomyces Species Reveals Their
RT Adaptation to the Marine Environment and Their Diversity at the Genomic
RT Level.";
RL Front. Microbiol. 7:998-998(2016).
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:OEV10459.1}.
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DR EMBL; LJGW01000294; OEV10459.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E7L2Q3; -.
DR PATRIC; fig|518642.10.peg.3649; -.
DR Proteomes; UP000176005; 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:SF34; PENICILLIN-BINDING PROTEIN 1A; 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 53..76
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 106..282
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 473..650
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..744
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..801
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OEV10459.1"
SQ SEQUENCE 818 AA; 88142 MW; AC9D17D8EDFCA1C2 CRC64;
RPGGGAGGAG GGRGSGPYGR GRRGFEPPPR KRFIDYPRWN KHGMRRWVPS WKLVLGSFAG
FLGLIIGLSG IALAMVGKPN VNEATKQQKN VYYWSDNTQM VVAGGGDQNR QIVPLAQIPK
AMQSAVISAE NESFYDDPGV DPIGIVRAVG RMALGGDTQS GSTITQQYVK NAYLDQSQTL
TRKFKELFIS IKVGATDEKD EILEGYLNTG YYGRGAYGIQ AAAQAYYRKD AKELNASQCA
FLSATLNGPN LYDPAGGVGS AATPDKNLER AKNRWSWTLD RMVKTGRLSS SDRAKYTSFP
RPKPPRKSTE LKGQKGYMVE TVNNYITANS NISEGRLKRG GLRIHTTFDK KKMAEMEAAV
ERVRKANIDP KKRNVDKYVQ FGGASVKPKD GAIVAMYGGE DATTHFTNNA DYTGVQVGST
FKPFVLAAAM RDGVRDPNGP EVQGRDARTP VSPKSVYNGD NKLKLRNYDR SIWRNEKGKE
WRQRNDGNES RGRISLREAM QYSVNTPYIQ LGMDVGVDKV RQSALDAGLN EDSLARSTPT
LSLGTSAPSA IRMANAYGTF ASSGMKSEPY SVTRVEENGE DLYNHQKQVK SAFEARVADN
VTNVLETVVQ DGTGTTARQL GRPAAGKTGT TDDNKSAWFT GYTPQLSTSI GMWRVNDKAK
TQRFQKMYGV GGQDSIHGAS FPAEIWTKYM TGALQGSAAK PFPTPEPIGE PVFGAGASPS
PTPTPSDTPS EDPSQDPSQP PTQSPSPTES CDNPFTCNDQ GQDGGNDQGQ TGGNDQGQTG
GNDQGQTGGN DQGQDGGTDN GNDNGGLFGG PGGTRERD
//
