ID A0A370B798_9ACTN Unreviewed; 820 AA.
AC A0A370B798;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=DVH02_19530 {ECO:0000313|EMBL:RDG36532.1};
OS Streptomyces corynorhini.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2282652 {ECO:0000313|EMBL:RDG36532.1, ECO:0000313|Proteomes:UP000253741};
RN [1] {ECO:0000313|EMBL:RDG36532.1, ECO:0000313|Proteomes:UP000253741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AC230 {ECO:0000313|EMBL:RDG36532.1,
RC ECO:0000313|Proteomes:UP000253741};
RA Dunlap C.;
RT "Streptomyces species from bats.";
RL Submitted (JUL-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:RDG36532.1}.
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DR EMBL; QQNA01000153; RDG36532.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A370B798; -.
DR OrthoDB; 8865355at2; -.
DR Proteomes; UP000253741; 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 Reference proteome {ECO:0000313|Proteomes:UP000253741};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 51..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 104..277
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 380..637
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 690..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..764
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 820 AA; 84630 MW; 7DB7537AAA9E5DBE CRC64;
MSDEPQQQGW APRDPSAQGA PGDPAPAGDG VSARKAKRLA RKRRRTGWRR LFPTWRMLLG
AFVLGALVLV GGFVLGYKMV PIPAANAAAT AQSNVYLYAD GTQIARDGEV NRENVSLSQV
PETVQRAVLA AEDRGFYSEP AVDPQGMARA AWNTVSGKGT QGGSTITQQY VKNYYLGQEQ
TVVRKAKEFF IAIKLNREAS KEQILQGYLN TSYFGRNAYG IQAAAQAYYG KDIEDINTAQ
GAYLASLLNA PSEFDVVVHP ENKPAALARW NYVLDGMVKE NWLSASTRAA TTFPRPGEVR
TSSTGLSGQR GYLVQAVKDY LTSHRIIDEN TLATGGYRIT TTLERKKQDA FVKAVKDKVT
SQLSEERAAD RNVRVGGASI DPESGKVVAM YGGIDYTKQY VNNATRRDYQ VGSTFKPFVF
ASAVQNGSET QDGRTITPNT LYDGDNQHMV DGPDGPTGYA PSNEDDVDYG PITVRTATDK
SVNAVYAQMA EDVGPSAVRK TAVALGLPPH TPDLTASPSI ALGPATASVL DMAEAYATLA
NHGAHGTYTL VGKVTKNGTK VALPARSGKQ VISREAADTT TSMLRSVVDG GTGTAAQAAG
RPAAGKTGTA EDDKAAWFAG YTPDLATVVA VMGADPKTAA QKPLYGALGQ QRVNGGGAPA
QIWGAYTAAA LRGSEAQDFD LQLQEGADVV ASPDTGESGR PDRPGTSTSP STPQGQTQGQ
SDGPTQGTTG TATGGGQSAD TTQGQTGGTA ADGGRTQGQT DGGTGTDGGA GADGGTGTAT
AGADTAGSAA DGGGGGGAAS GGADTGATAG AGAPPDLVLP
//
