ID V6KXL7_9ACTN Unreviewed; 791 AA.
AC V6KXL7;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=N566_16015 {ECO:0000313|EMBL:EST36882.1};
OS Streptomycetaceae bacterium MP113-05.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae.
OX NCBI_TaxID=1380770 {ECO:0000313|EMBL:EST36882.1, ECO:0000313|Proteomes:UP000017915};
RN [1] {ECO:0000313|EMBL:EST36882.1, ECO:0000313|Proteomes:UP000017915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP113-05 {ECO:0000313|EMBL:EST36882.1,
RC ECO:0000313|Proteomes:UP000017915};
RA Valde M., Degnes K.F., Sletta H., Ruckert C., Kalinowski J., Zotchev S.B.;
RT "Streptomyces bacterium from a marine sponge: physiological
RT characterization and genome-based analysis of secondary metabolite
RT biosynthesis potential.";
RL Submitted (SEP-2013) 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:EST36882.1}.
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DR EMBL; AWQV01000529; EST36882.1; -; Genomic_DNA.
DR AlphaFoldDB; V6KXL7; -.
DR STRING; 1380770.N566_16015; -.
DR PATRIC; fig|1380770.3.peg.2783; -.
DR HOGENOM; CLU_006354_6_0_11; -.
DR Proteomes; UP000017915; 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:UP000017915};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 50..76
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 105..273
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 376..639
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 675..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..736
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..771
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 791 AA; 83297 MW; 658B9A6DE8185B0C CRC64;
MDGKCLPKMS DEPHRDTGPY EPDGGWTSGE EPDAGETGER RSGPRRLLPT WRMVVGAVLT
VILVISGGMV AGYLLVDIPE PNPHAVSQSN VYLYSDGSRI AVDGEYNRET VPLTEISRGA
RRAMLAAEDR DFYSEPAVNL KAMSRAAWNM LTGGDTQSGS TITQQYVKNY YLTQEQTVTR
KVKEFFIAIK LDKEVSKDEI LQGYLNTSYF GRNAYGIQSA AQAYYGKDAG ELTAAEGAYL
ATLVNAPSAY DTRAHPENKD RVLARWNYVL RGMVEEGWLS KAKRKATEFP EPGPVKPSTS
LSGQRGYLVH AVDDYLTGHG VIAENRLASG GFTIRTTIDR KKQDALVDAV DEKLVSRLDE
KNNKVDTYVR TGGTSIDPRT GEVVAMYGGQ NFVEQYTNTA TAREYQVGST FKPFVFTSAL
DNGSTTQDGQ PITARTVYDG TSGRAVEVDG RDTRFAPENE DEVNYGRVTV SEATDKSINA
VYAQMGVDVG VENVRETATA LGIPADVMDP KVGGSISLGV SPASTVDMAE AYATLANHGM
HRDHTLVTKV TRGSETVDLP NRKEKRAVPR EAADTTTAVL KSVVEGGTAT AAQSAGRPAA
GKTGTAEDDK AAWFAGYTPD LATVISVVGK NPKTQAQESL YKAAGLERVN GGGPPAEIWG
AYTAAALAGE PVQSFDLDTR GPVLPTAPPT EDADPTGPPA TDRPTEEPPT QAPTTPGDPT
PPTGTPDPPT GDPSVPPDPT AGGTVDGGTT ESPTGGGTTE GTTTGGSTAG GEGPGGTSDG
DGGQSTGAGG G
//
