ID R2TF16_9ENTE Unreviewed; 776 AA.
AC R2TF16;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=UAW_01345 {ECO:0000313|EMBL:EOH98749.1};
OS Enterococcus haemoperoxidus ATCC BAA-382.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1158608 {ECO:0000313|EMBL:EOH98749.1, ECO:0000313|Proteomes:UP000013858};
RN [1] {ECO:0000313|EMBL:EOH98749.1, ECO:0000313|Proteomes:UP000013858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-382 {ECO:0000313|EMBL:EOH98749.1,
RC ECO:0000313|Proteomes:UP000013858};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A.M., Gilmore M.S., Lebreton F., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Enterococcus haemoperoxidus BAA-382.";
RL Submitted (FEB-2013) 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:EOH98749.1}.
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DR EMBL; AJAR01000012; EOH98749.1; -; Genomic_DNA.
DR RefSeq; WP_010761553.1; NZ_KE136479.1.
DR AlphaFoldDB; R2TF16; -.
DR STRING; 155618.RV06_GL001435; -.
DR PATRIC; fig|1158608.3.peg.1321; -.
DR eggNOG; COG0744; Bacteria.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000013858; 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:SF29; PENICILLIN-BINDING PROTEIN 1A; 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 Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 38..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 90..266
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 360..619
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 687..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 776 AA; 84874 MW; B3534EC93FDD38A8 CRC64;
MTTDEIGSRA ARHGHTPVSN GTENTPSNGG KKPKKKRILL KIFLGLVLLG ILGLLAGVGL
FWSYAKDAPK LEDDKLSATV SSKLYDANNE VFEELGAEKR EMIKPTDVPQ LLKDAVVSVE
DKRFYKHSGV DPIRILGSAF SNFKTGGLQG GSTLTQQLIK LSYFSTKEKD QNLKRKAQEA
WLAMQLEKEK SKEEILTYYI NKVYMANGLY GMETAAQAYY GKPLAELSLP QTALLAGMPQ
APNDYDPYVK PDVAKERRDV VLYTMKENDK ITQKEYDDAK ATPIADGLQP LKQSNENRKI
VDNYIREVIA EVESMGKNPY TDGLDIHTNL DMNAQKRLYD IINSDTYVEY PDPEFQVAST
VIDVKTGQVK AQIGGRNIPD DVQLGSNLAI ETDRDVGSTM KPIADYGPAI ENLNYSTGRI
MMDQPTTYEG TNIEVTNADM QYYGALTMRK AIMYSRNTTA IRTFDAVGSD KSAAFLKDLG
IEFKDFVAAN AISSNTSELG GNKYGVSSLK LAAAYAAFAN MGVYNKPYYV SKVVYQDGSE
DVTETESKRA MKDSTAYMMT DMLKDVISGG TAFNAGVPGL IQAGKTGTAN YTDDDLVKIG
ASASSSIAPD STFVGYTPHY AVSVWTGYKQ RLTPIPYEYW GTASDVYREM MTYLSEGVSN
DDWVMPDSVI RSGSELYVKG AYEEQLLPSN TGNTSSSSWE NPVSSEPGTT SSSTVPSQTE
PSSTQPSEPP VSSTQQTEPP ASTTPTEVLP SSEPPQESST PPVIQNNATR RRSSPG
//
