ID U5YNJ2_9ACTN Unreviewed; 768 AA.
AC U5YNJ2;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
OS Streptomyces sp. WM6372.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1415555 {ECO:0000313|EMBL:AGZ93893.1};
RN [1] {ECO:0000313|EMBL:AGZ93893.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=WM6372 {ECO:0000313|EMBL:AGZ93893.1};
RX PubMed=24297932; DOI=10.1073/pnas.1315107110;
RA Yu X., Doroghazi J.R., Janga S.C., Zhang J.K., Circello B., Griffin B.M.,
RA Labeda D.P., Metcalf W.W.;
RT "Diversity and abundance of phosphonate biosynthetic genes in nature.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20759-20764(2013).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KF386865; AGZ93893.1; -; Genomic_DNA.
DR RefSeq; WP_053690982.1; NZ_LGDB01000184.1.
DR AlphaFoldDB; U5YNJ2; -.
DR PATRIC; fig|1415555.3.peg.4032; -.
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 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..634
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 678..768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 768 AA; 80467 MW; 84308C2C95B1D053 CRC64;
MGKKRSGAGL TGPQQAAKFL GVSVLSGVVL AGIAIPGAGA LGLAAKGTVE GFDEIPANLK
TPPLSQRTTI LDAEGGLIAT VYSRDRQVVP LTAISPYMQK AIVAIEDSRF YEHGAIDAKG
ILRAVNRNAQ EGGAAQGAST LTQQYVKNVF VEEAGDDETK VREAQEKSLG RKIRELKYSI
QVEEELGKKK ILENYLNITY FGQQAYGIES AAQRYFSKPA KDLTLDESAL LAGVVQSPSR
FDPVNDAQEA MKRRNVVLQR MVDMKDISQA EADEAKKKPV TLKVTRPKNG CITAVKGAGF
FCDYVRNTFL TDPVFGKTRE ERAKLWNQGG LTVRTTLDPQ SQESVNESIK DHVNQDDKVA
TAVTLVQPGT GRVLAMGQSK PYGFGKNETQ INFSVDKRMG GSNFGFPTGS TFKPFVAAAA
LEKGVSPGKT YPSPHDMEYP SPVETCGDKP WVNTSHDRVE NESESERGPY GMQDAMAKSV
NTYFVEMISE NGLCPVTEMT TKLGVIPADG TKLPEVPAIA LGTEGMSPLT MANAYATFAN
RGVYCTPVAL ESITDAHGKA LAVPKSQCDR VMSEKTADTV NTLLLGVIDS GTGTAAGLTD
RQNAGKTGTT DSRYNAWFVG YTPNMAGATW VGSGGAKQVS MENITIGGQY YDKVYGGGLP
GPIWKQAVSG ALSGREAPTF TTVGIPESGG APTGGGRPST PNPNPNKPGK PGKPGGDGKP
GGRPGGQTAA GATGGPTGGL TGGATGGATG GGTPTDPFPG GVIGGLED
//
