ID A0A3M8BFD3_9BACL Unreviewed; 683 AA.
AC A0A3M8BFD3;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, 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=EDM57_00845 {ECO:0000313|EMBL:RNB61667.1};
OS Brevibacillus gelatini.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=1655277 {ECO:0000313|EMBL:RNB61667.1, ECO:0000313|Proteomes:UP000268829};
RN [1] {ECO:0000313|EMBL:RNB61667.1, ECO:0000313|Proteomes:UP000268829}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100115 {ECO:0000313|EMBL:RNB61667.1,
RC ECO:0000313|Proteomes:UP000268829};
RA Dunlap C.;
RT "Phylogenomics of Brevibacillus.";
RL Submitted (OCT-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 -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
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:RNB61667.1}.
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DR EMBL; RHHS01000005; RNB61667.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M8BFD3; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000268829; 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 NCBIfam; TIGR02074; PBP_1a_fam; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF11; PENICILLIN-BINDING PROTEIN 1B; 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 Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 62..237
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 329..595
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 683 AA; 76310 MW; 7B04B7BC3D4C1C92 CRC64;
MEVIREPSLL RYLRWIKKFV KFSILSLLCL SFAILLLILY LRSQPLPETF VKQTTTIYAA
NGEVLDTMHR GENRISVPLQ EIAPALINAT IAIEDRSFRE HYGFDWKRLA MAAYVDVINM
DMRQGASTIT QQLARNLYLT MDKTWERKIK EALLAIQLEL NYSKDEILEM YMNQIFYGHS
AYGAQAAAQT YFGKDAKDLS VAESAMLAGI PKGPTYYSPF VDFERAKSRQ KLILEAMERE
GMLTAKEVEQ AYAEPIKLKD RTAENVTEQA PYFRDYIANL VKNKYGIDEE KFIHGGLKIH
TTLDPVMQKK AEEIVASTLP KDNPNLQAAL IAMDPATGHI KAMVGGRDYK TSQYNRVLGK
RQPGSSFKPI MYLAALQNGY TPLTMMKSEP TVFTYDNNKQ YIPSNFGGRY ANAMINMREA
IKTSDNIYAV KTIDFLSPQK VVEQAKALGI TSPLQAVPSL ALGTSPVSPL ELNTAYAAIV
NKGEAVQPIA ITSIEDSEGN ILVQEKTQKT RVADPVASAL LVNMMQSVFE RGGTGYRVAN
ELNRPVAGKT GSTDYDAWLS GFTPQLVTTV WVGYDKNQKV DDVKEGNFSK KIWASFMESA
LKGQPPALFE MPAGVVSVYI DPASGKLATE HCPNPQLFYF ASGTEPQDYC TDHIPANQEP
TPLPPPDSST FWQRMGSWWK PAE
//
