ID A0A0N0SY62_9ACTN Unreviewed; 768 AA.
AC A0A0N0SY62;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=ADL01_33455 {ECO:0000313|EMBL:KOV60255.1};
OS Streptomyces sp. NRRL WC-3618.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1519490 {ECO:0000313|EMBL:KOV60255.1, ECO:0000313|Proteomes:UP000037738};
RN [1] {ECO:0000313|EMBL:KOV60255.1, ECO:0000313|Proteomes:UP000037738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL WC-3618 {ECO:0000313|EMBL:KOV60255.1,
RC ECO:0000313|Proteomes:UP000037738};
RA Noorani M.;
RL Submitted (JUL-2015) 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:KOV60255.1}.
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DR EMBL; LGDW01000462; KOV60255.1; -; Genomic_DNA.
DR RefSeq; WP_053745773.1; NZ_LGDW01000462.1.
DR AlphaFoldDB; A0A0N0SY62; -.
DR PATRIC; fig|1519490.3.peg.7294; -.
DR OrthoDB; 8865355at2; -.
DR Proteomes; UP000037738; 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:UP000037738};
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 77..261
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 362..669
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 688..768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..761
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 768 AA; 80949 MW; 737FA0802533F2D8 CRC64;
MPNKRSGGGL SATQQAAKFL GVSVLAGAVM AGIALPAAGA LGLAAKGSVE GFDEIPANLK
RPPLSQRTTI LDAKGGQIAT VYSRDRTVVE LKDISPYLQK AIVAIEDSRF YEHGAIDLKG
VLRALNKNAQ SGGVAEGAST LTQQLVKNVF VEEAGDDPTK VAQAQQQTIG RKIKELKYAI
QVEEQLGKKK ILENYLNITF FGQQAYGAEA GSRRYFSKAA KDLTLPQAAL LAGIVQSPTR
YDPVNDPAEA IKRRNTVLKR MSEVGDITPQ AAEAAKKAPL GLKVSQPKNG CIAAVQGASF
FCKYVEKEFL ANPVFGKTRE DRTKIWDQGG LTIRTTLDPQ SQASVQASIK QHVNKSDSVA
TAVTLVEPGT GKILGMGQSK PYGYGKNETE INYSVGSDRG GSNFGFPTGS TFKPFVAAAA
LEEGRPAIQE YSSPYQMTYP SPVQTCSGKP WTNLTDEKLE NESESEKGPF RLRKAMELSV
NTYFVQMISD IGLCPVAKMT DALHVRQGNG DKLPEVPAIA LGSKGISPLT MASAYAAFAS
RGMYCTPVAI ESITQKANGV EKSLEVPKST CSRAMSEKTA DTINTLLQGV VDSGTGKEAG
LTDRDNAGKT GTTDARKNAW FVGYTPALSG AVWVGSAMQN VKMTNISIGG QFWELVYGGK
VPGPIWKDAM TGALVGKDSG KFNIIPIIEP APPKPADKGD GRGDGDNGDN NGNNIAGATN
GGDNGGNTFP NPTFSFPEGF VQGNDNGGNN GNGNGNGNGG NGFTGGFP
//
