ID Q834C6_ENTFA Unreviewed; 803 AA.
AC Q834C6;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN OrderedLocusNames=EF_1740 {ECO:0000313|EMBL:AAO81514.1};
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185 {ECO:0000313|EMBL:AAO81514.1, ECO:0000313|Proteomes:UP000001415};
RN [1] {ECO:0000313|EMBL:AAO81514.1, ECO:0000313|Proteomes:UP000001415}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583 {ECO:0000313|Proteomes:UP000001415};
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R., Read T.D.,
RA Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L., Brinkac L., Beanan M., Daugherty S., DeBoy R.T.,
RA Durkin S., Kolonay J., Madupu R., Nelson W., Vamathevan J., Tran B.,
RA Upton J., Hansen T., Shetty J., Khouri H., Utterback T., Radune D.,
RA Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
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};
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DR EMBL; AE016830; AAO81514.1; -; Genomic_DNA.
DR RefSeq; NP_815444.1; NC_004668.1.
DR RefSeq; WP_002382391.1; NZ_KE136528.1.
DR AlphaFoldDB; Q834C6; -.
DR SMR; Q834C6; -.
DR STRING; 226185.EF_1740; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR EnsemblBacteria; AAO81514; AAO81514; EF_1740.
DR KEGG; efa:EF1740; -.
DR PATRIC; fig|226185.9.peg.1636; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_2_0_9; -.
DR Proteomes; UP000001415; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 3.40.50.12800; -; 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 PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF32; PENICILLIN-BINDING PROTEIN 2A; 1.
DR Pfam; PF00912; Transgly; 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:ARBA00022670};
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:UP000001415};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 44..69
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 100..271
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT REGION 782..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 803 AA; 88472 MW; ECA248FE73911CDC CRC64;
MYHFIEVKLL KNNSSNNKQK PTTSSGGNVF LLILNVIIRV FQSLVVFGVI LIVLGGSLGL
GIGMGYFAFL VEDTQPPTKE ELQKEISDIT EVSKMTYADG TPIANIKSDL IRTRINGDQM
SPLLKKAIIS TEDEYFEEHH GVVPKALVRA LISDATGIGG SSGGSTLTQQ LVKQQILTDE
TTFKRKANEI LLALRIEKYF SKDEIVTTYL NVSPFGRNNK GENIAGVEEA AKGLFGKSAK
DLNLPQAAFI AGLPQSPIVY TPYTNTGALK DDLSLGMKRK DFVLFSMYRE KAISQKEYEE
AKAYDLKKDF LPTEQANVNT EGYLYYTVLD KAVEIVMDLD MKKAKVNRDD LDQVGLDQYE
EQARREIQSQ GYTIQSTIDQ NIYNTMQTAV ANYGYLLDDG TADVNGNTMI ETGNILMDNA
TGRILGFIGG RNFDINQNNH AFNADRQVGS TIKPISVYGP AIDQGIIGSE SRLANYPTTY
ADGREFVNST NVDLNQFVTV RNALNWSFNI PVVHVNNELR KKMGDDNFSY NHYLSKMNYP
ASDAWAYESA PLGSVETNVV TQTNGFQALA NKGKYQKAYM IEKITDNSGH VVYEHKDEGT
QVYSPATASI MNDLLRSVVD SANTTKFKPT LAGLNPHLAS ADWVGKTGTT DEFKDSWLIV
STPTVTLSSW AGHDLPAPMT MTSGDNNGNY MANLANALYY ANPELFGIGQ KFELDPSVIK
SKVSEFTGEK PGSITYNGAK FNTPGKTTTS YYAKDGAPQS TYKFGIGGTD SNYASYWGNL
APRATTNNNN NNNKNNDNKK NNN
//
