ID A0A1E7DLP7_9BACI Unreviewed; 651 AA.
AC A0A1E7DLP7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=BA724_12945 {ECO:0000313|EMBL:OES43983.1};
OS Domibacillus iocasae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Domibacillus.
OX NCBI_TaxID=1714016 {ECO:0000313|EMBL:OES43983.1, ECO:0000313|Proteomes:UP000095658};
RN [1] {ECO:0000313|EMBL:OES43983.1, ECO:0000313|Proteomes:UP000095658}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29979 {ECO:0000313|EMBL:OES43983.1,
RC ECO:0000313|Proteomes:UP000095658};
RA Verma A., Pal Y., Ojha A.K., Krishnamurthi S.;
RT "Domibacillus iocasae genome sequencing.";
RL Submitted (JUN-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};
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:OES43983.1}.
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DR EMBL; MAMP01000024; OES43983.1; -; Genomic_DNA.
DR RefSeq; WP_069939760.1; NZ_MAMP01000024.1.
DR AlphaFoldDB; A0A1E7DLP7; -.
DR STRING; 1714016.BA724_12945; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000095658; 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; 6.20.370.110; -; 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 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 Membrane {ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000095658};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 65..237
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 333..605
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 651 AA; 72043 MW; A92646436750DBCF CRC64;
MKVVIRLIQN LWRKFHLTQI VILLAAIVVL AGLGTGFYFM KSADVETLKQ GLSQSTIIYD
RNGEKASKLS ANRTDSVSIE KMPEHLQEAI VAVEDNRFYE HGGFDVKGIF RAFFTNIMAG
SRVQGASTIT QQLTKNALLS PEKTYRRKVE ELFLAIEIEK VYKKEEILEM YLNTSYFGNG
AWGVQNASKK YFGKDVSELT LAESSMLAGM VKAPSRYNPI DNMDNALERR QVVLNQMVKY
SYITESEANE TANIDITLRD TSGDPLKGKY AHYADAVINE AISRYGLTQD DLLTQGYNIY
TSMDQDVQAG LEGVYENSSV FPETVNGEDS QSAAVLVDPK TGGVLGVVGR RGEHIFRGFS
FATQMKKSPG STIKPLAVYT PALEEGYEPT DMLEDKEMSF GEGEDPYSPT NYGGMYEGEL
PMYRAVEKSA NIPAVWLLDQ IGVSKGVNAL KRFGLEVENA KLGMALGDIT PGVSPLQMAE
AYTAFSNDGV RKETFFIQKI VGPDGEVEPE WEPEEVKVTS KEITDQMTAM LLGVVERGSG
ERAQVDEVDI AGKTGSTQVP IEGIEGTEDQ WFVGYTPNLV GAVWVGVEEV SKTNYLTTNS
SDGAVPLFGE VVSEILPYIG ETSFDVEAID SNAKQEEHWY DGIIEKWNEW F
//
