ID A0A3R9TYE8_9ACTN Unreviewed; 771 AA.
AC A0A3R9TYE8;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=EF917_11340 {ECO:0000313|EMBL:RSS04067.1};
OS Streptomyces sp. WAC00469.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2487415 {ECO:0000313|EMBL:RSS04067.1, ECO:0000313|Proteomes:UP000269080};
RN [1] {ECO:0000313|EMBL:RSS04067.1, ECO:0000313|Proteomes:UP000269080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WAC00469 {ECO:0000313|EMBL:RSS04067.1,
RC ECO:0000313|Proteomes:UP000269080};
RA Culp E., Yim G., Waglechner N., Wang W., Pawlowski A.C., Wright G.D.;
RT "Unmasking the antibiotic production potential of Actinomycetes through
RT CRISPR/Cas9 inactivation of ubiquitous gene clusters.";
RL Submitted (NOV-2018) 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:RSS04067.1}.
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DR EMBL; RPRX01000029; RSS04067.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R9TYE8; -.
DR OrthoDB; 8865355at2; -.
DR Proteomes; UP000269080; 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 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:UP000269080};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 75..261
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 362..635
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 682..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..704
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 771 AA; 81246 MW; 54664DC76143380F CRC64;
MPNKRSGGGL SPTQQAAKFL GVSVLAGVVL AGIALPAAGA LGLAAKGSVE GFDEIPADLK
RPPLSQRTTI LDSQGRQIAQ VYSRDRTVVP LKDISPYMQK AIVAIEDSRF YQHGAIDLKG
VLRALNKNAQ EGGVAQGAST LTQQYVKNVF VEEAGDDPTK VAQATQQTLG RKIKELKYAI
QVEQELGKKK ILENYLNITF FGQQAYGIEA ASQRYFSQHA KDLTLPQAAL LAGLVQSPSR
YDPVNDPAEA TRRRNVVLQR MAEVGDISQE EADKAKKEPL GLKVTPPRNG CITAVDGAAF
FCKYVEQVFL NDPVFGKTRA DRAKIWNQGG LTIRTTLDPQ AQAAVQASLK KHVYQSDSVA
AAAVLVEPGT GKIVAMGQSK PYGYGKDQTE INYAVGSDRG GSNFGFPTGS TFKPFVAAAA
IEGGKPPTQE YSSPYKMPYP SPVQACDGKQ WTNTDHNEVE NESTSEHGPY ALKEAMAKSV
NTYFVQMISD IGLCPVVKMT DKLHVVQGNG QKLPQQPSIA LGAIGISPLT MASAYAAFAS
RGVYCTPVAI ESITQSTGDQ EKSLPVPKTT CTRAMSQKTA DTVTTLLQGV IDSGTGKQAG
LSDRDNAGKT GTTDERKNAW FVGYTPNMAG AVWVGSASQQ VKMTNIRIGG VLHGLVYGAD
VPGPIWRDAM TGALRGKAAP SFHLVDIPDG GDKGKGRDRG NDDTHPGNQG TGGNTGDGGG
LFGGLFGGGR GGGTGGAGNG GAFPTPTFSL PPGFFQGQDG GFRGQRGHGD G
//
