ID Q8DS45_STRMU Unreviewed; 784 AA.
AC Q8DS45;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 115.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN Name=pbp1b {ECO:0000313|EMBL:AAN59595.1};
GN OrderedLocusNames=SMU_1991 {ECO:0000313|EMBL:AAN59595.1};
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007 {ECO:0000313|EMBL:AAN59595.1, ECO:0000313|Proteomes:UP000002512};
RN [1] {ECO:0000313|EMBL:AAN59595.1, ECO:0000313|Proteomes:UP000002512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159 {ECO:0000313|Proteomes:UP000002512};
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H., Lin S., Qian Y., Li S., Zhu H.,
RA Najar F., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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; AE014133; AAN59595.1; -; Genomic_DNA.
DR RefSeq; NP_722289.1; NC_004350.2.
DR RefSeq; WP_002263431.1; NC_004350.2.
DR AlphaFoldDB; Q8DS45; -.
DR STRING; 210007.SMU_1991; -.
DR KEGG; smu:SMU_1991; -.
DR PATRIC; fig|210007.7.peg.1772; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_2_0_9; -.
DR OrthoDB; 9766909at2; -.
DR PhylomeDB; Q8DS45; -.
DR Proteomes; UP000002512; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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 NCBIfam; NF038274; strep_PBP1B; 1.
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 ECO:0000313|EMBL:AAN59595.1}; 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:UP000002512};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 55..76
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 109..281
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 420..654
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 784 AA; 86356 MW; 35F00D0DCE18D52B CRC64;
MSLLNKIKTK FKRNIKKPHF KKIDVTKFNL KILKRADYLD VASVFLRTFK LLSDFAYILI
LLIAFMGIGM GFGYLASQVE SVKIPSKVNL VNQVSTFTRI SKMTYSDKSI ISTIDTDLLR
TPIESRNISD NVKKAVIATE DENFKTHKGV VPKAVFRATL ASVLGLGENS GGSTLTQQLL
KQQVLGDDPT FKRKTKEIIY ALALERYIGK DSILTNYLNV SPFGRNNRGQ NIAGIEEAAK
GIFGVAAKDL TIPQAAFLAG LPQSPITYSP YTADGKFKTK KDMEYGLKRS QNVLYNMYRT
GVLSKVDYES YKKYDLRKDF KRPQASQTDS HDYLYYSVFE EAQKVMYDYL IKRDHVSSQD
LKNDKTKAAY KEKALREIRL GGYTIATTIN KMVYNAMQMA VAQHGASLDD GTGNVEVGNV
LMDNSTGAIL GFVGGRDYKS NQNNHAFDTA RSPGSSIKPL LAYGPAIDQG LMGSSSMLSN
YPTTFSSGQK IMHAGDEGTA MVNLQEALDV SWNIPAYWTY QMLLQKGVDV PDYMEKMGYN
IPEYSIESLP LGGGVETTVA QQTNGYQTIA NGGVYQKQYM IDKITDSKGK VIYQHEPKPV
RVYSQATASI LNDLLKGPIS SGKTTTFKDK LKGLNSDLAG AEWTGKTGTT DDYTDVWLIL
STPKTTLGGW AGHDNNASLD KMSGYNNNAQ YMAYLVNAIN QADPNILGTN QRFSLDPSVI
KADVLKSTGL KPATVNVNGK NISLSGETTT SYWAKNGPGD TVYKFAIGGS DSDYQKAWAS
IGGK
//
