ID A0A089M2Q5_9BACL Unreviewed; 615 AA.
AC A0A089M2Q5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=PSTEL_24375 {ECO:0000313|EMBL:AIQ65773.1};
OS Paenibacillus stellifer.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=169760 {ECO:0000313|EMBL:AIQ65773.1, ECO:0000313|Proteomes:UP000029507};
RN [1] {ECO:0000313|EMBL:AIQ65773.1, ECO:0000313|Proteomes:UP000029507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14472 {ECO:0000313|EMBL:AIQ65773.1,
RC ECO:0000313|Proteomes:UP000029507};
RA den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT "Comparative genomics of the Paenibacillus odorifer group.";
RL Submitted (AUG-2014) 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};
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DR EMBL; CP009286; AIQ65773.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A089M2Q5; -.
DR STRING; 169760.PSTEL_24375; -.
DR KEGG; pste:PSTEL_24375; -.
DR HOGENOM; CLU_006354_2_2_9; -.
DR Proteomes; UP000029507; Chromosome.
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: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; SSF53955; Lysozyme-like; 1.
PE 4: Predicted;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000029507}.
FT DOMAIN 66..232
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 328..607
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 615 AA; 65039 MW; 0E5C08146168EEA1 CRC64;
MRRLPYAAFD LAVVLTGACV LLLFGLRLYG EQTLAQQADK LLLPQSTVLL AADGSVMSRI
PIPGGGYREN AESGELPPLL LETVMAVEDR RFYEHKGLDY RGLARALASN VSAMRVEQGG
SGITQQLARS LFLSRKQTVA RKLKEAAIAM ALERHLSKAE ILRLYLNETY LGRGQYGVKR
AAFYYFGVRD LKELTPAQVA LLAGIPKGPS IYNPVDRPEL AVKRMQEVLG IMKSNGLITA
AEERRALQIG LHGAALSPGS AAEYSAAGYV DAALQEASAR TGIPLAKLRE GGYTVTTGLN
PSAQRAAEAA FRNPANFPPD AGGERVQGAV VILDSRTGEV KAMVGGRDET GGGLNRAVSA
ARQPGSAIKP ILVYGPALES GRFTPDSLLP DRPASYGGYS PGNIKGVYRG TVTMNTAVER
SINAPAVWLL NEVGVTPALA FAAKLGIELP AEDRQLAIAL GGTHGGVSPL QMAQAYGVFA
SGGRFSTGHL VREVRDGSGH LLYQCTPESQ QVISARTAEM MTAMLVGAVN EGTGRKARLS
GRMVAGKTGT TQLDIQGVPS AANRDAWFAG YTKGWSAAVW IGFDRTDRNH YMTDGGGTAA
ALFAAIMGPA LNALP
//
