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Database: UniProt
Entry: D5AK92_STRGZ
LinkDB: D5AK92_STRGZ
Original site: D5AK92_STRGZ 
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
//
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