ID G7SD54_STRSU Unreviewed; 807 AA.
AC G7SD54;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=SSUD12_0118 {ECO:0000313|EMBL:AER18465.1};
OS Streptococcus suis D12.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1004952 {ECO:0000313|EMBL:AER18465.1, ECO:0000313|Proteomes:UP000008845};
RN [1] {ECO:0000313|EMBL:AER18465.1, ECO:0000313|Proteomes:UP000008845}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D12 {ECO:0000313|EMBL:AER18465.1};
RX PubMed=22026465; DOI=10.1186/1471-2164-12-523;
RA Zhang A., Yang M., Hu P., Wu J., Chen B., Hua Y., Yu J., Chen H., Xiao J.,
RA Jin M.;
RT "Comparative Genomic Analysis of Streptococcus suis reveals significant
RT genomic diversity among different serotypes.";
RL BMC Genomics 12:523-523(2011).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002644; AER18465.1; -; Genomic_DNA.
DR RefSeq; WP_014637308.1; NC_017621.1.
DR AlphaFoldDB; G7SD54; -.
DR KEGG; ssk:SSUD12_0118; -.
DR PATRIC; fig|1004952.3.peg.115; -.
DR HOGENOM; CLU_006354_2_0_9; -.
DR Proteomes; UP000008845; 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:AER18465.1}; 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 Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 37..60
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 89..260
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 400..633
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 760..807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 807 AA; 87185 MW; C2549336224F4185 CRC64;
MATKSDKQDF KKKISALGLG DVVGVFLRTL KLLFNSVAVL VFLFGLFGAG IGIGFVVSLF
DDVKIPKTEE LVAKVSEVSR ISTVTYSDGS LVSEVNSDLL RVPITSEEVS NYLKQAVIAT
EDETFETHNG VVPKAVLRAA LGSVGLGSSS GGSTLTQQLI KQQLVGDAPT FTRKANEIVS
ALALERNMTK EEILTIYLNV SPFGRNNQGR NIAGVEAAAQ GIFGKPAKDL TVPQAAFIAG
LPQSPIVYSP YASDGTRKSD EDMVYGIERY QDVLFNMYRA SFLTKEEYET YKAYDIKQDF
IAPAPVMADT KDYLYYEVME EAQEVMFDYL VKRDKVSEND LKNDETKASY EELAKQELSQ
GGYTIKSTVD QGIYAAMQSV VANYGSVLDD GNEYVETGSV LIDNATGAIL GFVGGRDYAT
NQNNHAFDTL RSPASTIKPL LAYGIAIDQG LIGSASILSD YPTNFSSGQP IMYGSGRGTG
MMNLQTAIDR SVNIPAFWTY KMMRNAGVDA KVYMDKMNYH IPMYDIESVP LGGGVEISVL
TNTNAYQTLA NGGVYNKHYI VESITASDGT VVYQHEAAPV QVYSKATASI MNQLLRQVVN
SGYTTTFKSR LSGLNPQAAS SDFVGKTGTS NEVNDVWLML STPRVTLGTW AGNDDNSEMY
VWTGYHNNSQ YVAHMVDALY NVNADMFAGK FELDSSVIAS SVVASTGQRA GTTQVNGRQV
TVGGAMTTSY WAKNGAPVTS YNFMVGGTDS DRAQAWNTII GSQTPTSSSS TQRSSSTRSS
TSSSANNTNQ SSETQTATSE QANNDSP
//
