ID G5JRF6_STRCG Unreviewed; 750 AA.
AC G5JRF6;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN Name=pbp1A {ECO:0000313|EMBL:EHI73896.1};
GN ORFNames=STRCR_0743 {ECO:0000313|EMBL:EHI73896.1};
OS Streptococcus criceti HS-6.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=873449 {ECO:0000313|EMBL:EHI73896.1, ECO:0000313|Proteomes:UP000004322};
RN [1] {ECO:0000313|EMBL:EHI73896.1, ECO:0000313|Proteomes:UP000004322}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HS-6 {ECO:0000313|EMBL:EHI73896.1,
RC ECO:0000313|Proteomes:UP000004322};
RA Stanhope M.J., Durkin A.S., Hostetler J., Kim M., Radune D., Singh I.,
RA Town C.D.;
RL Submitted (JUL-2011) 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:EHI73896.1}.
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; AEUV02000002; EHI73896.1; -; Genomic_DNA.
DR RefSeq; WP_004226434.1; NZ_AEUV02000002.1.
DR AlphaFoldDB; G5JRF6; -.
DR STRING; 873449.STRCR_0743; -.
DR eggNOG; COG0744; Bacteria.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000004322; Unassembled WGS sequence.
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; 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; NF038272; strep_PBP1A; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF29; PENICILLIN-BINDING PROTEIN 1A; 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 48..72
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 96..272
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 366..624
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 704..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..742
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 750 AA; 81641 MW; 6AC6A9306214DD26 CRC64;
MKNFNFKFPD LKGIGNNLSD RIKSIGKSEG EHGRKLTPKQ KSWKFFKYFL GIIASLAIVG
IIAGGLLFAY YASSAPSLSE RQLVATNSSI LYDKNGSEIA DLGAEKRISA KTDSIPVNLV
NAITAIEDHR FYKHRGIDIY RIIGAAWHNM TRTSTQGGST LDQQLIKLAY FSTNNSDKTL
KRKAQEAWLS IQMEKKYSKE EIMTFYVNKV YMGNGYYGMQ TAAKGYYGKS LTDLSIPQLA
LLAGLPNAPT LYDPYTNPEQ AKKRRDTVLS EMYKVGNIDK KTYDSAIATD VGDGLIPQTE
KSSYDAYLDN YIKEVVNQVS EKTHADVYSA GLKVYTNVDS TAQQRLYDIV NSDDYVAYPD
DKMQIATTVI DVTNGNVVAQ IGARHQDAAV SMGSNQAVLT DRDWGSTMKP ITDYAPAIEN
GVYNSTGASI SDSPYNFPGT STPVYDWDRK YMGTMSIQTA IQQSRNIPAV KSLYAVGLDK
AQSFLSGLGI NYPELQYSNA ISSNTSSSDQ KYGASSEKMA AAYAAFANGG TYYEPLYINK
IEFSNGKDQT FSSNGSQAMS PETAYMMVDM MKTVLQAGTG TKAAVPGAIN AGKTGTSNYS
DDELAQVEAD TGLYNASVGT MAPDESFVGI TPMYSMAVWT GYKSRFTPVY GTGLDVAAEV
YQAMSSFLFQ TYGSGSTDWT MPDGVYRSGG YVAKSGYSNN YSYSTSSSSY GYSSSSDSQT
QSSSSSSDNS SSSSSQTDQN NSDSDDNDSE
//
