ID A0A3N6G0B4_9ACTN Unreviewed; 747 AA.
AC A0A3N6G0B4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN Name=pbpF {ECO:0000313|EMBL:RPK78077.1};
GN ORFNames=EES45_18915 {ECO:0000313|EMBL:RPK78077.1};
OS Streptomyces sp. ADI97-07.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1522762 {ECO:0000313|EMBL:RPK78077.1, ECO:0000313|Proteomes:UP000281409};
RN [1] {ECO:0000313|EMBL:RPK78077.1, ECO:0000313|Proteomes:UP000281409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ADI97-07 {ECO:0000313|EMBL:RPK78077.1,
RC ECO:0000313|Proteomes:UP000281409};
RA Guerrero-Garzon J.F., Zehl M., Urban E., Schneider O., Ruckert C.,
RA Busche T., Kalinowski J., Zotchev S.B.;
RT "Streptomyces spp. from the marine sponge Antho dichothoma: analyses of
RT secondary metabolite biosynthesis gene clusters and some of their
RT products.";
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:RPK78077.1}.
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DR EMBL; RPGY01000095; RPK78077.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N6G0B4; -.
DR Proteomes; UP000281409; Unassembled WGS sequence.
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 Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000281409}.
FT DOMAIN 76..261
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 362..643
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 678..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 747 AA; 78817 MW; 9F2EBA9B6447D288 CRC64;
MPMKRSGGGL TTTQQAAKFL GVAALSGAVL AGIALPAAGA LGLAAKGTVE GFDEIPSNLK
TPPLSQRTTI LDNEGGPIAT VYSRDRTVVP LKDISPYMQA AIIAIEDSRF YEHGAVDLKG
ILRAMNRNVQ EGGAAQGAST LTQQYVKNVF VEEAGDDPDK VAEATQQTLG RKVRELKYAI
QVEEELGKKK ILENYLNITF FGQQAYGVEA ASQRYFSKHA KDLKLEEAAL LAGLVQSPSR
YDPVNDTEEA TKRRNTVLQR MAAVGDISQS EAGKAIASKI ELKVRKPQNG CITAVSGSGF
FCDYVRKTIL TDPAFGKTEE ERSKLWNLGG LTVKTTLSPR AQKAANEAAT SKVHKDDKIA
ASVVQLQPGS GKILSMGQSR PYGLDQKQNE TVLNLAVSNK MGGSTFGFQV GSTFKPITAA
AALEKGISPA QSFSSDWKIS VPMSSYRDCS GSPTGGGTWD LQNEMESEKG AYDMTSALGK
SINTYFAKLE QKAGLCETVT MAKKVGYERG DGEPVSDKHP SITLGGTEST PLAMAAAYAT
FANRGTYCTP IAIESITDAN DKKLEVPKSS CSRAMSEATA DTLNQMLKGV VEDGTGTLAG
LTDRDNAGKT GTTNDRVDAW FVGYTPNLST AVWVGADVGK KVPMYNITIG GQYYEKVCGG
CLPGPIWKTA MTGALSASET PTFNPISVPR AKEKEDKEQD GGREEDNDGD NDGNGRPGGG
NAIGGITLPP GVIGGNDGGR GGGGNGP
//
