ID A0A3S2TUY6_9BACI Unreviewed; 967 AA.
AC A0A3S2TUY6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=EM808_05290 {ECO:0000313|EMBL:RVT64931.1};
OS Niallia taxi.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Niallia.
OX NCBI_TaxID=2499688 {ECO:0000313|EMBL:RVT64931.1, ECO:0000313|Proteomes:UP000288024};
RN [1] {ECO:0000313|EMBL:RVT64931.1, ECO:0000313|Proteomes:UP000288024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M5HDSG1-1 {ECO:0000313|EMBL:RVT64931.1,
RC ECO:0000313|Proteomes:UP000288024};
RA Tuo L.;
RT "Bacillus sp. M5HDSG1-1, whole genome shotgun sequence.";
RL Submitted (JAN-2019) 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:RVT64931.1}.
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DR EMBL; RZTZ01000002; RVT64931.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S2TUY6; -.
DR Proteomes; UP000288024; 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; 3.90.1310.40; -; 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 Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR001264; Glyco_trans_51.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
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:UP000288024};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 35..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 97..280
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 417..661
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 900..967
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 909..967
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 967 AA; 106648 MW; DA77056489E29C56 CRC64;
MNERPKWKNY LHGFLSFFTN KKTVKRARIT YEVSWNIILI FIILLIVGGA FAGGIGAGYF
ASLVKEEPIR SYKTMQKDIY NYEETSELYF ADNVYLGKLP TDLEREEVKI KDVSPHLVDA
IVSTEDENFY KHDGVVPKAI MRALFQEVSN SSTQSGGSTL TQQLIKNQIL TNEVSFERKA
KEILLALRLE KFFSKEEILE AYLNVSTFGR NSSGRNIAGV QAAAQGIFGV EAKDLTLPQS
AFIAGLPQSP FGYTPFTQDG TVKENLEPGL ERMKTVLARM YNQHKISKED YDKAAAYDIT
KDFASPVVSP IEKYPWVTYE IENRATQIIA EMLAKEDGYN AKDLEEDEVL YDQYTELADR
QIHQNGYEIH STINKKIYDK FTEVVDKYPY FGPDKPQTVT DSETGEKKTI MEPVETGAIL
IDNKSGAIIS FVGGRDYGRE ATNHSTSPRP NGSTMKPLLV YGPAIELGTL SPGTVLPDVP
LALDPARPGT VWPNNYDFQF HGLVTARVAM AKSYNVPAVK AYAQILPQKP ANYLEKMGFT
TLTEGDYANR STSIGGLTNG VSVEENTNAF ATFANGGNFV DAYMIDKIVD KDGKVIYKHK
TEKVKVFSPQ TSYLTIDMMR DVINQGTATA VKSRLKFSSD WAGKTGTTQD FKDSWFVATN
PNVSFGVWTG YDTPKSLVSS GTMSYSMRNN YLWADLMNAA YDVDSKLVDP SESFTMPGGI
VRRSVCSLSG LLASEGCSKA GLVTTDLFKS SSVPNKTDDS IVTGKYVQIG NTKYMALDST
PSEFSETGVI LNPDYIEKLF GIKVSDPSDL IRNNTALKNV VVPSNKITDN GKAPNAPKVS
NSGSTIAWSK SGEKDVIGYR VYQNGKKVAS IKASDTLSFK AGSGSYVVKA VDIAGKESSN
SNKIEVASKQ SSKAKEDDKK ANKATAKKTE EDNKAEASKE KKQENNDSDN KKEDSSADNK
EEKTDNT
//
