ID A0A317KZD8_9BACI Unreviewed; 705 AA.
AC A0A317KZD8;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=DLJ74_17505 {ECO:0000313|EMBL:PWU67019.1};
OS Gracilibacillus dipsosauri.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Gracilibacillus.
OX NCBI_TaxID=178340 {ECO:0000313|EMBL:PWU67019.1, ECO:0000313|Proteomes:UP000245624};
RN [1] {ECO:0000313|EMBL:PWU67019.1, ECO:0000313|Proteomes:UP000245624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD1 {ECO:0000313|EMBL:PWU67019.1,
RC ECO:0000313|Proteomes:UP000245624};
RA Deutch C.E., Yang S.;
RT "Genomic analysis of Gracilibacillus dipsosauri DD1 reveals novel features
RT of a salt-tolerant amylase.";
RL Submitted (MAY-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:PWU67019.1}.
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DR EMBL; QGTD01000019; PWU67019.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317KZD8; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000245624; 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:UP000245624};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 57..230
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 320..578
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 705 AA; 79798 MW; F239B448414F9760 CRC64;
MRRRRRRRKK RWLKWGFFMF LVGASSFVFL IGASFILGPP SLERAENTIY YSSDQEVIGE
EYGSEKRYWV DLDEIDDKLE KAIVWTEDQH FYDHLGFDFK RLAGAIVKDI QTMSLKEGAS
TITQQYARNL FLSHEKTWKR KLYEAFYTIR LEMYYDKDEL LEGYLNTIYY GHGAYGIEAA
SKYYFNKSAK DLSWAEATLL AGIPKGPSIY SPFHDLENAK QRQAFILENL LENDVIDQAT
YDAAINEKLN FSDDRMIVKN SIAPYFQDIV VEELKSLLDL NMEEIRSGGY KVYTTLETDQ
QLALQTASES VLNNGEIQVG AVAMDPDTGG ITALVGGQNY EASSFNRAVQ AKRMPGSSFK
PFLYYAALEN GMTAATTMMS KPTTFALENG QSYQPSNFNN YYANAPITMA QAVALSDNIF
AVKTNLYVTP ERFARIAKEK FAIESPLEPV ASLALGTEVV SVKEMVTGYS IIANGGKKVN
SHVIEKVTDS QGNVIYQYEE PKEEAGGFPF FSKKETNQLL KPALTYILTD MMKGMFDQEL
NGYMSVTGAS IADQLTHDYA GKSGTTESDS WMVGFSPELV AGVWIGYDDN RSIEKVSEEH
FSKEIWANFM EKAHESIPVT ESKPPENIIE VPIDLNTGLL ATDECGEAYT MPFIKGTQPS
QYCTSHLEEI NEENSEELKE ITEDDPFLED WWDWLWFGDN STVTE
//
