ID A0A2U2ZDI8_9ACTN Unreviewed; 823 AA.
AC A0A2U2ZDI8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-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=DIZ27_12085 {ECO:0000313|EMBL:PWI10350.1};
OS Streptomyces sp. NWU339.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2185284 {ECO:0000313|EMBL:PWI10350.1, ECO:0000313|Proteomes:UP000245372};
RN [1] {ECO:0000313|EMBL:PWI10350.1, ECO:0000313|Proteomes:UP000245372}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NWU339 {ECO:0000313|EMBL:PWI10350.1,
RC ECO:0000313|Proteomes:UP000245372};
RA Adegboye M.F., Lobb B., Babalola O., Doxey A.C., Ma K.;
RT "Draft genomes of two novel cellulolytic Streptomyces strains isolated from
RT South African rhizosphere soils.";
RL Submitted (MAY-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:PWI10350.1}.
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DR EMBL; QFRK01000008; PWI10350.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U2ZDI8; -.
DR OrthoDB; 8865355at2; -.
DR Proteomes; UP000245372; 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:UP000245372};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 60..82
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 111..279
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 381..635
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..786
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..823
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 823 AA; 87321 MW; 54C7C30B4C16D190 CRC64;
MSDEPQPQQH GQGWAPREPR AAGTPQRGTG TGTGTGTGSG TGGKRVRTGW RRFVPTWRMV
LGGFLVAALL LVGGFFLGYS LVHIPSANAL ATQEANVYLY ADGSVLARDG VVNRESVSLD
RISAEAQHAM LAAEDRDFYT ESAVDPQAMI RAAWNTATGK GKQSGSTITQ QYVKNYYLRQ
EQTVTRKVKE FFIAIKLERE QSKDEILEGY LNTSYFGRNA YGIQAAAQAY YGIDAQDLDA
PRAAYLAALV NAPSQYDVIA HPENRPAVES RWNYVLDGMV QQGWLNEAER TGLKFPEPKE
TTTSTGMSGQ RGYIVRTVKD HLIRNKILDE EELDAGGHRI TTTLHKDKQD AFVDAVNDNL
IDRLDPENRK VDTYVRAGGA AIDPRSGKVV AMYNGIDYVK QYTPNATRRD YQVGSAFKPF
VFASAVENGS TTQSGQPITP NTVYDGTNER TVQGWPGERY APANEDDRSY GHITVREATD
KSVNAVYAQM AADVGSDKVQ QTAIDLGIPA TTPELTASPS IALGVATASA LDMAEAYATL
ANHGEHRAHT MIEKITKDGK KTVPLPERKT RRAVSREAAD TTTAVLRGVV QNGTASAAQG
AGRPAAGKTG TAEEDRAAWF AGYTPELATV VSVMGQDPVT AAQKELYGAM GLSRINGGGP
PAEIWAQFTR EALKDEPVSD FDLRLQRGAE HTAPPTASAD PSSSTTDDAS QAPGTDESAN
RNPGQDEDGT EGGTQGRTDE DTTGDIPTGG GTSDSGTTPA GDTTGVTGDG TGNTGNTGNG
GTDGANGTDG TGGPPGTGTD TGRGGQGSQD GLTGFIQQSA RRQ
//
