ID S1NDU2_9ENTE Unreviewed; 832 AA.
AC S1NDU2;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=OMK_01280 {ECO:0000313|EMBL:EOT41111.1};
OS Enterococcus dispar ATCC 51266.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1139219 {ECO:0000313|EMBL:EOT41111.1, ECO:0000313|Proteomes:UP000014127};
RN [1] {ECO:0000313|EMBL:EOT41111.1, ECO:0000313|Proteomes:UP000014127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51266 {ECO:0000313|EMBL:EOT41111.1,
RC ECO:0000313|Proteomes:UP000014127};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Russ C., Gilmore M., Surin D., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Enterococcus dispar ATCC_51266 (Illumina only
RT assembly).";
RL Submitted (MAR-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:EOT41111.1}.
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DR EMBL; AHYR01000005; EOT41111.1; -; Genomic_DNA.
DR RefSeq; WP_016172456.1; NZ_KE136354.1.
DR AlphaFoldDB; S1NDU2; -.
DR STRING; 44009.RV01_GL002184; -.
DR PATRIC; fig|1139219.3.peg.1240; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_2_0_9; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000014127; 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; 3.40.50.12800; -; 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 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:UP000014127};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 32..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 90..262
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 398..640
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 772..832
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 832 AA; 91259 MW; 10BF948585CF5B8B CRC64;
MPKKQKHHNE PFSDRKKGWF YFNISLRVLH SLILVGISCL IIGGALALGI GAGYFAYLVE
DTPAPNKATM QKELGDVSQT SKLTYADNSS IATIRSDLFR TSVKSDQISN LLKKAIIATE
DEYFYEHNGV VPKAVVRALL SEATGFGGGG GSTLTQQLVK QQVLTSETTF KRKANEILLA
MEVEKFFSKD EIVTMYLNVS PFGRNNKGQN IAGVQEAAKG IFGKDAKDVN LPQAAFIAGL
PQSPIVYSPF DNTGKLKENV TAGLERKDFV LFSMYRNHDI SKKEYEAAKK YDLKKDFLKQ
QTQNNDDHGF LYYTVMNEAK SIVAQQLAKD DGVSTQDYEK KKTKEAYLEK AQNELINGGY
TVKSTIDKKI YDAMQKGVAE YGYMLDNYSG DKIEVGNVMM DNATGKILGF IGSRDFSDNQ
NNHAFDTSRA AGSTIKPILV YGPAIDQGLI GSQTRISDYP AKWKAGEDAG KEIVNATNKG
SKTFQTVEDA LAESTNITAY HVYQELQEKK SADFVYDNYL AKMNFPANNS WNVESAPLGP
MDVTTVQQTN GFQALANGGV YQQGYLIEAI TDSQGKAIYK HENKPVRVFS KATASIMNNL
MRNVLSQGIT TPFKSTISNL NWYLGQADWV GKTGSSDYYR DSWLIVSTPK VTIGSWSGMD
SQKEKNDDGA GTRTGNYMAY LINRIYMANP EIFGTDQKFK LDDSVKQETV AKATGELPGS
ISYNGATVQV PNDTTTSLWA KNGPADSNYR FGIGGTDANY ADYWNKIYAK SKTSTQQKNS
NNTSSNSTTS GNSNNATTAN NNGSNSNNAN TTANNTNGNN SSNGTTNNNN GQ
//
