ID A0A197SLR1_9ACTN Unreviewed; 895 AA.
AC A0A197SLR1;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=A8W25_15085 {ECO:0000313|EMBL:OAR23824.1};
OS Streptomyces sp. ERV7.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1322334 {ECO:0000313|EMBL:OAR23824.1, ECO:0000313|Proteomes:UP000078470};
RN [1] {ECO:0000313|EMBL:OAR23824.1, ECO:0000313|Proteomes:UP000078470}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ERV7 {ECO:0000313|EMBL:OAR23824.1,
RC ECO:0000313|Proteomes:UP000078470};
RA Lavstsen T., Jespersen J.S.;
RL Submitted (MAY-2016) 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:OAR23824.1}.
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DR EMBL; LYOY01000040; OAR23824.1; -; Genomic_DNA.
DR RefSeq; WP_067162173.1; NZ_LYOY01000040.1.
DR AlphaFoldDB; A0A197SLR1; -.
DR STRING; 1322334.A8W25_15085; -.
DR OrthoDB; 8865355at2; -.
DR Proteomes; UP000078470; 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:UP000078470};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 118..141
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 170..348
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 551..735
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 785..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..520
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..827
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..895
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 895 AA; 95508 MW; 876034CDB7EB8925 CRC64;
MSEHRRKPPE SQGGGRAAAR RAAQQPSGRR AAPARDSVTE SPSGSYGEQR PAGGRAEARR
AAQRGGRRRA AEPGGGGPAG PGGRRGGTGP GNRRPGKKRF IDYPRFNKRG WRRWMPSWKL
VSGLCLGFLS TLVIVIGIAY WSVSVPNVAQ AATAENNVYY WSDGSQMVAT GGEVNRQIIG
YEKIPAAMRY AVISAENKTF ETDSGVDPQG IARALVNMAK GGHTQGGSTI TQQYVKNARL
DDQSQTLTRK FKELFISIKV GATKKKSEIM AGYLNTAYYG RGAYGLQAAA RTYYSKDAQN
LDASQCAFLA SLLKGATYFD PAGATEIDPA ATPQQNTKNA MNRWAWILDE EVKDGHLSAA
ERAKYKTFPM PDKPKKNAQL SGQIGYLVSL SKAYFVNNNT QGITAGDLDQ GGYEIHTTFD
KKKVQALEDV VKKVRKKNID PKKRPEYDTF VQFGAASVDT KSGAIKALYG GEDATKHFTN
NADQTGAQVG STFKPFVLAA AMEYGKRDPK GPKDQGESER TPVSPKSIYS GMNKLKIKNY
DGSVWTNEKG EQWLQTNDGN ESYNKPSYAI DLRYAMQESA NTPYVQLGMD VGTDKVRDVA
LAAGLRKDSL ASSSVPSFSI GTSSPSAIRM AGAYSTFATS GMHHDPYSVE KVNKRGRAVY
QHDDKATRAF SAAIADNVTD VLKNVVEKGT GTNAKLSGRE VAGKTGTTDG NRSAWFVGYT
PQLSTAVSMY RLDDNETNKK REFLKMFGTG GQEKIHGASF PSTIWHDYMD QALNGVPAVD
FPTPEAIGDK VYGGGMSPSP TPSPSPSGSP SPSGSPSPTP SLTPSPSPKP TKSCGKWDWN
CGGPGGPGGT DAGTDAGTDQ GTTTGDTSGP SGSPSPTRSK PGNASQGNIF GGPTG
//
