ID A0A370GE77_9BACI Unreviewed; 690 AA.
AC A0A370GE77;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=DFR59_106140 {ECO:0000313|EMBL:RDI41981.1};
OS Falsibacillus pallidus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Falsibacillus.
OX NCBI_TaxID=493781 {ECO:0000313|EMBL:RDI41981.1, ECO:0000313|Proteomes:UP000255326};
RN [1] {ECO:0000313|EMBL:RDI41981.1, ECO:0000313|Proteomes:UP000255326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25281 {ECO:0000313|EMBL:RDI41981.1,
RC ECO:0000313|Proteomes:UP000255326};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (JUL-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:RDI41981.1}.
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DR EMBL; QQAY01000006; RDI41981.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A370GE77; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000255326; 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 Reference proteome {ECO:0000313|Proteomes:UP000255326};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 17..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 61..236
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 328..582
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 690 AA; 77741 MW; D49EFDA2C133944E CRC64;
MEVVRPRLKR TIKYVRAFLF IGGFFTILFM LFLAGMLIYI KIQGPPPLSV QQSSLMYAND
GTIIGESNNG QKRYWVDLDE ISPYLTEATV AIEDRNFYEH HGFDYKRIAG ALLADVKAMA
KVEGASTISQ QYAKNLYLTR DKTWNRKISE ALYTIRLEWN YSKNQILEGY LNTIYYGHGA
YGVEAASRYY FNKEAKDLSL GEAAMLAGIP KGPSIYSPFV SYERAKERQK TILSEMASQH
LISKKQAQTA MSEKLVFTGK FPIQHAEIAP YFYDAVKQEL KNKVGLDERT IEFGGLRIYT
TLDIKQQKIA EEVVKETVSD HSDIQVGFAA MNPKNGYVTA LIGGRDYVKS SYNRAVQALR
QPGSTMKPIL YYAALEKGFT PSTTMRSEMT TFHFDEKRPD YTPHNFNNNY ANGEITLAQA
LALSDNVVAV KTHLFLGIDT LVNEARQFGL TSKLARVPSL ALGTSGVHVT EMVNAYSMIA
NGGKKIEPTF ITKVEDYEGN VIYENDSSHD QVLDKDTDFV LTHMMEGMFD PKLNGYASVT
GTTILNKITR PYAGKSGTTD SDSWMIGFAP QLTAGVWTGY DNGQPITLTA DKLYAKNIWI
RFMESALKDE PIKAFKPTKG VVGVKVDPEN GKLATEDCPR ARLTYFKEGK EPTEYCQLHL
SNPIEKPDEP QAEKKAQEKK EPWYKKIFPW
//
