ID A0A329LKC7_9BACL Unreviewed; 1065 AA.
AC A0A329LKC7;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=DQG13_04830 {ECO:0000313|EMBL:RAV04547.1};
OS Paenibacillus sp. YN15.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1742774 {ECO:0000313|EMBL:RAV04547.1, ECO:0000313|Proteomes:UP000251619};
RN [1] {ECO:0000313|EMBL:RAV04547.1, ECO:0000313|Proteomes:UP000251619}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YN15 {ECO:0000313|EMBL:RAV04547.1,
RC ECO:0000313|Proteomes:UP000251619};
RA Niu L.;
RT "Paenibacillus sp.YN15.";
RL Submitted (JUN-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:RAV04547.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QMFA01000004; RAV04547.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A329LKC7; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000251619; 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 CDD; cd00063; FN3; 1.
DR Gene3D; 1.10.3810.10; Biosynthetic peptidoglycan transglycosylase-like; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR001264; Glyco_trans_51.
DR InterPro; IPR013783; Ig-like_fold.
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:SF32; PENICILLIN-BINDING PROTEIN 2A; 1.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
PE 4: Predicted;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW ECO:0000313|EMBL:RAV04547.1}; 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:UP000251619};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 26..55
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 87..276
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 402..661
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 801..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 916..990
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 921..957
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1065 AA; 116824 MW; 6030C3FAF5DF6984 CRC64;
MTQTNTSVWK RIGAFFRKRA VRRTGLVLFM TVKWMIISII IACFAAGGAA FGYLASVLKD
EPIRSEAFIR EQIEQNMLTG FVYFNDQTPI GQLRTEEDRR MATMADIPQM LIDATLAIED
NSFNEHIGVD VNGLVRAVKQ KLLNEDVQTG GSTITQQVAR RVFLTLDRDI TRKFKEIFLA
VRMERFLTKD EILLAYLNKI PYGNGSNGYT VYGIKAAAKG LFDMDDLNGL NIAQSAYLAG
LPQLPSDYSA FSGKGEFDSA AFNRAVKRQQ LVLRRMLEEN KITQQQYDGA LAFDLKGSLA
KSSQKAYTTY PYLMMEVERK ASEAMVKAQY PDLKLDTDSK KAAFNEAQKD ALNQLLRGGY
HIYTTIDKTI YDSMQTIAQN PKNFTANLKN VQKEKDGIEQ IGAVMIDNKS GAILGMMEGR
DFYTEQLNHA TQAYRQPGST MKPIAAYIPA LEKGAIQPAT VIDDAPIILP DGQKGVHIPM
NWNNKFQGLV TAREALNQSY NIPALKLFLY QVGIKEAWDY AAKMGITSIT KEDAVAQTGV
IGGLYKGVNV EEMTNAYTTI PNQGVFYDAY LIDKIVDSTG KVVYQHERKP SRVYSEQTAY
LMTDMLRTVI TSGTAPEIKN NFKYYKNMAV SGKTGSTQDD ADAWFMGFTP DITLGVWAGY
DQPVNKLVKG TGTKRALNIW AQVMNEAVEK RPELFPTKAF TKPADIVEMT VSSVSGKLPN
ELTAAAGKSV TDLFNKKYVP TQEDDVMVKM KYITYNGVNY IPQPGTPDDF LSEQVVIRRE
KSVSKLLSEI KDAMEKLPED NRKPLDLFVP ADAGDDAPSE TDPRTDDGTI PGQPGGIAVT
RSGDVNRISF APVAAPDIVG YRLYRTTDGH SFVRAGTPQV LMTNPAEPVF TDPAPGGEAY
GYYVSAVDVA GRESVPSQPV FADGRNHSQA NQTGNGGLLP SGSVSPGNGT PNKGASPGGS
LTPGKPTPAP AAPQKEPSEP KGLKAKSKGV SLQLTWSANP RAEAVSEYKV YYSDTENGAY
KLIGTSEGTE FIYFAATNDG YYKLSAVNEL GESPLTGAVH YTQSQ
//
