ID D5AK92_STRGZ Unreviewed; 737 AA.
AC D5AK92;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 24-JAN-2024, entry version 70.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN OrderedLocusNames=SSGZ1_1801 {ECO:0000313|EMBL:ADE32257.1};
OS Streptococcus suis (strain GZ1).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=423211 {ECO:0000313|EMBL:ADE32257.1, ECO:0000313|Proteomes:UP000002359};
RN [1] {ECO:0000313|EMBL:ADE32257.1, ECO:0000313|Proteomes:UP000002359}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GZ1 {ECO:0000313|EMBL:ADE32257.1,
RC ECO:0000313|Proteomes:UP000002359};
RX PubMed=19016627; DOI=10.1086/594370;
RA Ye C., Zheng H., Zhang J., Jing H., Wang L., Xiong Y., Wang W., Zhou Z.,
RA Sun Q., Luo X., Du H., Gottschalk M., Xu J.;
RT "Clinical, experimental, and genomic differences between intermediately
RT pathogenic, highly pathogenic, and epidemic Streptococcus suis.";
RL J. Infect. Dis. 199:97-107(2009).
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; CP000837; ADE32257.1; -; Genomic_DNA.
DR RefSeq; WP_012027868.1; NC_017617.1.
DR AlphaFoldDB; D5AK92; -.
DR SMR; D5AK92; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR GeneID; 8154155; -.
DR KEGG; ssw:SSGZ1_1801; -.
DR PATRIC; fig|423211.3.peg.1773; -.
DR HOGENOM; CLU_006354_2_2_9; -.
DR OMA; VDLWFIG; -.
DR Proteomes; UP000002359; Chromosome.
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; 6.20.370.110; -; 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; TIGR02074; PBP_1a_fam; 1.
DR NCBIfam; NF038276; strep_PBP2A; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF32; PENICILLIN-BINDING PROTEIN 1F; 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 Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 105..272
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 373..630
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 737 AA; 81546 MW; 5341A0127AC572EA CRC64;
MDDLQHQPIE VPEDFQIDHE DRPSRRHRGN RGSIDKPKKK SRIPEPIRKF WRRYQLTKIL
IILMVLTVLT VGGYLFFLAK TANVGDLQQA LKATTIIYDK DGAEAGTLSG QKGTYVELDA
ISDNLENAVI ATEDRSFYKN SGINYQRTIL AALTLGRSGG GSTITQQLAK NAFLTQDQTI
SRKAREFFLA LEINKKYSKQ EILTMYLNNA YFGNGVWGVE DASQKYFGIP ASNLTLEQAA
VIAGMLKGPE IYNPYYSLEN AVNRRDTVLQ NMVNAGYIDQ ATADAGFQVD LASQLSDTYT
GKQSNYSYPS YFDAVIAEAI ERYGLKESDI INNGYRIYTE MDQNSQASMQ VIFNDETMFP
TSSFDGTHAQ AASVALDPRT GGVRALVGRV NSSEDAVFRT FNFATQAKRS PGSTIKPLVA
YAPAVAAGWS IDMALDNHTE TYGDYTLHNY DYSTSDTIPM YQALALSYNL PVAYIVNTLG
IDKAFEYGQK FGLDMENVEK VLGVSIGSGV ETNPLQMAQA YATFANKGVM KDAHLITRIE
TASGKVLAEH RETSTKVIDR AVADKMTAMM LGTYTNGTGV TADTANYHIA GKTGTTETSF
DVNLVNDQWH IAYTPDLVIS QWVGFEQTDE NHYIDSSSYW KAPSVFQTVA NSILPYTAGS
KFEVENAYAQ NGIVEVAPDE AAQTESSLGQ EQVQEISEQA KNLIEQTKQN LIDAQLPERA
KTLWDNITSW FGELSNP
//