ID A0A1G8N563_9BACI Unreviewed; 717 AA.
AC A0A1G8N563;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, 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=SAMN05216352_111109 {ECO:0000313|EMBL:SDI75255.1};
OS Alteribacillus bidgolensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Alteribacillus.
OX NCBI_TaxID=930129 {ECO:0000313|EMBL:SDI75255.1, ECO:0000313|Proteomes:UP000199017};
RN [1] {ECO:0000313|EMBL:SDI75255.1, ECO:0000313|Proteomes:UP000199017}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P4B,CCM 7963,CECT 7998,DSM 25260,IBRC-M 10614,KCTC 13821
RC {ECO:0000313|Proteomes:UP000199017};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNDU01000011; SDI75255.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8N563; -.
DR STRING; 930129.SAMN05216352_111109; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000199017; Unassembled WGS sequence.
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:SF36; PENICILLIN-BINDING PROTEIN 1F; 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:UP000199017}.
FT DOMAIN 52..226
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 318..590
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 717 AA; 79725 MW; F6B5839A395CB7D9 CRC64;
MRNKWIIWGL AVFTFIILSA GIYLSSVVIG AAAIDEKKLV MNETTEIFDN NGEKLAELYI
EDRDLINIED IPDHVKQPFV AIEDIRFYDH QGIDPRAILR ALYRDILAGS KVEGGSTITQ
QLAKNAFLSS DKTLLRKTKE VLIAMGLERK FSKDEILGYY LNQVYFGHGA YGIKSAAELY
FDKAVEDLTT DEAALLAGIP KAPGNYSPVE DAERAKERRN TVLALMERHG FITAEEATAY
QGKTVPDSLN RSKETTAFYT YIDMMLEEAE NKYHLTPEEV YRGGYDIVVP MNKEMQQASY
DLFQEEAYFP EEAKDAEGAF FMMDHHSGGV AAVQGGREYV RRGLNRVKVK RQPGSVMKPL
AVYAPALESG EYHPYSLLKD EQMDFDGYSP KNYNGEYRGE ISMADAITES TNTAAVWLYD
QIGEKESSTW MEELGLQIED NGLAVALGGL TEGLSPMELA SAYTAFSNQG TKVNPYFIEK
ITDRNGEVIG QADPETKEVM SAQNAWYMTR LLENVVQEGT GTAGETVYPL AGKTGTTSFL
EIEGGTRDAW FAGFTPQWTG ALWMGYDKTT EDQHLQAGSS YPTRLFKEIL NDVPADDSVQ
TAFQQPEDVK DLEEPVEMAR VNDLSASLSL KGGGLFNVHL KWSAAADERV IYRVYEVNDG
EGEIIEEVEG DSEFTIEGVN VFNLQDYMVV PFNPQTEKEG EPSNVAEVSV GSLFGAG
//
