ID A0A1G8ZLY4_9BACI Unreviewed; 690 AA.
AC A0A1G8ZLY4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=SAMN05216243_2099 {ECO:0000313|EMBL:SDK16058.1};
OS Sediminibacillus albus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Sediminibacillus.
OX NCBI_TaxID=407036 {ECO:0000313|EMBL:SDK16058.1, ECO:0000313|Proteomes:UP000198694};
RN [1] {ECO:0000313|EMBL:SDK16058.1, ECO:0000313|Proteomes:UP000198694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.6502 {ECO:0000313|EMBL:SDK16058.1,
RC ECO:0000313|Proteomes:UP000198694};
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};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
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DR EMBL; FNFL01000003; SDK16058.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8ZLY4; -.
DR STRING; 407036.SAMN05216243_2099; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000198694; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000198694};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 65..238
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 329..606
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 659..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..680
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 690 AA; 77137 MW; CF73BD2BA35BA8D0 CRC64;
MISIVRQLLQ QINNRFLRWA TAFAFLAGAA CLFLVASIYA TAYILGPPSM TKGGNTVYYS
DSEQVIGEEH GPESRYWVKL EEISPIVIKA AITTEDKRFY SHHGLDLPRI ASAAWNDLIA
MSKVQGASTI TQQFARNLYL SHEKTWSRKL KEAFYAIRLE MHYDKDEILE GYLNTIYYGH
GAYGVEAASR YFFDKPANAL DIAEAALLVG IPKGPSYYSP FNHLDNAKER QQKILSSLHK
EKIISKEELF LAERKNLKLT EPEDRMEEQT APYFLDAALA ELQNILGIDR EAIRSGGYKV
YTTLNLDNQQ KMENVITSSV KENTKLQVGA VALSPHNGAV TAMVGGRDYS DSQYNRVTQA
KRMPGSSFKP FLYYAALENG YTAATSLLSK PTSFELEDGT VYQPSNYNGY YANEPITLAQ
ALALSDNVYA VKTNLFLGPE QLVNTAKKFG IDEDFQAVPS LALGTGAVTV KEMASAYSML
ANGGHEVEAF TIKKVTDTHG KLLYEREEAD QPPVLDPAKA FILTDLMTGM FDESLNGYMR
VTGVTIADQL SRPYAGKSGT TKTDSWMVGF SPDIVTSVWT GYDENKPIEN VKEQQVAKEI
WADFMEQAHE KLPFHTFSVP KGVVGAYVDP VSGELATPYC GQQRLMYFAK GTEPANYCSL
HQPEDPKEKP PEEKKEEKDS GWKRWFKWLS
//
