ID A0A1Z5ID21_9LACO Unreviewed; 768 AA.
AC A0A1Z5ID21;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=IWT30_01619 {ECO:0000313|EMBL:GAW99649.1};
OS Secundilactobacillus mixtipabuli.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Secundilactobacillus.
OX NCBI_TaxID=1435342 {ECO:0000313|EMBL:GAW99649.1, ECO:0000313|Proteomes:UP000198374};
RN [1] {ECO:0000313|EMBL:GAW99649.1, ECO:0000313|Proteomes:UP000198374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IWT30 {ECO:0000313|EMBL:GAW99649.1,
RC ECO:0000313|Proteomes:UP000198374};
RA Tohno M., Tanizawa Y., Arita M.;
RT "Draft genome sequences of new species of the genus Lactobacillus isolated
RT from orchardgrass silage.";
RL Submitted (NOV-2015) 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:GAW99649.1}.
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DR EMBL; BCMF01000007; GAW99649.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z5ID21; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000198374; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; 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:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase 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:SF29; 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:UP000198374};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 78..256
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 353..612
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 670..768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..768
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 768 AA; 83558 MW; 5FF8950B6A265969 CRC64;
MSSNQSNPQT RSEMHAERNR GSNGHHTFRR IFKWLFVLFL AAILLGAVVF FYYAEGAPSI
SQSALESDTS TKVYDSNNNV ISRLGAQNRD YVKSKNIPAQ LKSAVVSIED RRFYKNYGVD
PIRIISAAVH NVTGSSLGLQ GGSTLTQQLV KLSVFSTAKS DQTLKRKSQE AWLAIKVDQK
YSKQQILEFY INKVYMGNGV YGMQTAAHYY YGKSLTKLSL PEMAMIAGMP QSPTNYDPIH
HPKYATYRRN QVLDAMVANK QITASQATAA KAVGVQSDLA KTHPVSTINL TNQKYIDAYL
KEVYSELKSD GYNTNTDGLR VYTNLNMSAQ KHLYSIANSN NYVAYPSNKF QLGATMVNPN
NGKVVAMLGG RKTSNVSFGL NRAVQTDRSS GSTAKPIADY GPAIQYLKYP TYQPVQDTQY
YYPGSTRELN DFDNRHEGTI TMRKALVESR NIPAVRTLDA VGINRATNFL GNLGMTFNDK
LTLQNGIGLY ISTEQEAAAY AAFANGGTYY KPHLLDHVVT ADGKSHSYGV KGTRAMSPAT
AFMITDMLKG VITSTNGSGT AANISGLYQA GKTGTTAYPD DYASSVPSDA AMDSWFTGYT
KNYSLSVWTG YDKQFEQGHY LPYEQTKIAQ EIYRSEMSYV QQNASNTDWT APSDVVATRR
NGTTEYYVAG YPGDASTATN DGISSSTNAN DSTGNNEANT NSSSKSSSSS KSSSTSTEQR
PTGGNGGAGG GGNNDTQNTN SNSTETTPNT NNGDNTGRTN TATTKNGQ
//
