ID A0A1R1SNL0_9ACTN Unreviewed; 751 AA.
AC A0A1R1SNL0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=SPAR_08611 {ECO:0000313|EMBL:OMI39886.1};
OS Streptomyces sparsogenes DSM 40356.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1331668 {ECO:0000313|EMBL:OMI39886.1, ECO:0000313|Proteomes:UP000186168};
RN [1] {ECO:0000313|EMBL:OMI39886.1, ECO:0000313|Proteomes:UP000186168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40356 {ECO:0000313|EMBL:OMI39886.1,
RC ECO:0000313|Proteomes:UP000186168};
RA Coyne S., Seebeck F.P.;
RT "Genome sequence of Streptomyces sparsogenes DSM 40356.";
RL Submitted (MAY-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:OMI39886.1}.
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DR EMBL; ASQP01000126; OMI39886.1; -; Genomic_DNA.
DR RefSeq; WP_065963917.1; NZ_ASQP01000126.1.
DR AlphaFoldDB; A0A1R1SNL0; -.
DR STRING; 67365.GCA_001704635_07345; -.
DR Proteomes; UP000186168; 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:UP000186168};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 39..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 82..259
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 357..606
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..695
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..717
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 751 AA; 79711 MW; 3F9D28C620F672E6 CRC64;
MGRAEERRAR QKSARKARKG AKKGAKKTGI RRFFTWKMVL GYFLSLGLLL VGGFIALYIW
VDVPNANALA KAEANIYKYS DGSIMARTGK VNRESVPLSK IPKDVQHTFV AAENKDFYSD
PGVSFTGTAR GMINTLLGRG KQGGSTITQQ YVKNYYLSQE QTVSRKLKEL VISLKVDQQM
SKDDILAGYI NTSFYGRDAY GIQAAARAYY NKDVQKLSVG EGAYLAALLQ APSQYDYSVA
GPNGKRLVKQ RWNYVLDNMV QKHWLDPGKR EGMKFPKPLD PRPVPGMDGQ TGYFVEAAKQ
ELYKSGVSED ELAAGGWTIT LNIDKKKQKA LERAVRTQLT DDLKPKTRPV DKHAQVGAVS
VNPKNGAIVA MYGGAGATKH WMNNATREDY QPASTFKPLI LAAALENDST TRDGTKITAN
TIYDGDSGRP VKDASGNNVG FAPPNEDHKD YGPITVQTAM NNSVNSVFAQ MAQDVGLEKV
KKTATALGMN PKAGGFDVAP AMSLGVMGAS PQDMAGVYAT LDNHGEKVTP SIIKSAVKGD
QRAELPDTTG GEVISRTAAD SVTSVLTGVV DKGTGTAVRQ EGQAVAGKTG TSDDNKSAWF
TGYTPNLVTS VGMFGEGQGG KQVTLTGTGG GGRVNGGGYP AEIWAAYMKA ALDGQGSARF
DLDTDMGAAV PPPSSTSPTT PPTSESSEPT TSAPPTSETP TTPPTPTTTP PTTPPTSGGK
PSTGTTTPPT TPPTTPTDTR GVRLGPPGRH G
//
