ID A0A269WB14_9BACL Unreviewed; 1029 AA.
AC A0A269WB14;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-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=CHH75_04290 {ECO:0000313|EMBL:PAK55463.1};
OS Paenibacillus sp. 7541.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=2026236 {ECO:0000313|EMBL:PAK55463.1, ECO:0000313|Proteomes:UP000215741};
RN [1] {ECO:0000313|EMBL:PAK55463.1, ECO:0000313|Proteomes:UP000215741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7541 {ECO:0000313|EMBL:PAK55463.1,
RC ECO:0000313|Proteomes:UP000215741};
RA Kalinowski J., Ahrens B., Al-Dilaimi A., Winkler A., Wibberg D.,
RA Schleenbecker U., Ruckert C., Wolfel R., Grass G.;
RT "Isolation and whole genome analysis of endospore-forming bacteria from
RT heroin.";
RL Submitted (AUG-2017) 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:PAK55463.1}.
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; NQLZ01000005; PAK55463.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A269WB14; -.
DR Proteomes; UP000215741; 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; 1.
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:SF33; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; 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:PAK55463.1}; 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:UP000215741};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 84..273
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 388..639
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 795..816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 902..962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 907..923
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1029 AA; 113258 MW; 541B0EB1EA31CF8E CRC64;
MVEEKKQGPA KKKKAPTKRS FWRIMGSVFG WLFVLGMMGV LFVGGAVGGY VTSIVKEEPV
RSRSVIEQTI NENAITGFAY FRDGSPIGQL RTDEDRRPVN YEDIPQIVID AIVSIEDNRF
FTHKGVDFRG TARAVKERLL NEPTQTGGST LTQQLARLTF LSRDRTDNRK VKEILLSMRM
ERFLTKEQIV TGYLNKVPFG NGSSGYQVFG IKAAARGIFN INDLNELNIA QAAYLAGLPQ
LPSAYSAYNG QGNFDEEAFK RALNRQSRVL ASMLQEGKIT QAEYEEAKAF DIKSSLAPKT
QKAYVTYPYL MIEVERQASK ILMELAENDS ADEDSKAAKE AALVQLSTGG YKVYTTIDRT
VYRTMRAIAE DDSNFFPDSE EKGMEQTAAM MIDNKTGAIL GMIEGRDFYK EQMNYATQME
RQPGSAMKPV AAYLPALESG ALQPASIVDD SPIILKDYSK VYHIPKNSYS GYRGLMTARQ
ALNDSTNTVA LKLFNETIGI ENAWEFSKKL GINTLKESDY AASTGVLGGL STGVTVEELT
NAYSAIGNQG KFNDAYMIEK IVDSKGNIVY KHEAEPVQVF SEQTAYLMTD MLRTVITNGT
GSKVRDTYKK FNEIPVVGKT GSTQNYGDVW FMGYSPDITL GVWVGYEKPI HTLVGDQRRH
AQAIWARIMN EVTDAKPDLF PTSAFERPEG IVSKTVSAYS GKLPSSLTDR FVTDLFNQKY
VPTEVDDGIV KAKYITYRGV NYIPREETPE DMLKEQNVIK RPKPIDELIR ELEEALRVMK
GEKGSLESYL PADAKSGVPT KIDPRTDDGK APTPPKNVSY SAGSISFSPS GSPDVVGYRL
FKSLNGGAFV QDRVVLADET TVFTGLGSDS PFTAYYVVAV DVVGKTSEPS AIVGPLGIHM
PMPGDDEEDL DSFPDDTPGE SDGEEITDPA TGGQADTMIP PSPPGQPTLS ATPEGFSATW
PGNAGQEEVI RYNVYFSPDN GNFQQIGSSQ STEFYYTSGN PISGYFRITA VNAYGESPPS
SAVFFEKSE
//
