ID E8V5K4_TERSS Unreviewed; 823 AA.
AC E8V5K4;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN OrderedLocusNames=AciPR4_0705 {ECO:0000313|EMBL:ADV81538.1};
OS Terriglobus saanensis (strain ATCC BAA-1853 / DSM 23119 / SP1PR4).
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Terriglobus.
OX NCBI_TaxID=401053 {ECO:0000313|EMBL:ADV81538.1, ECO:0000313|Proteomes:UP000006844};
RN [1] {ECO:0000313|EMBL:ADV81538.1, ECO:0000313|Proteomes:UP000006844}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC BAA-1853 / DSM 23119 / SP1PR4
RC {ECO:0000313|Proteomes:UP000006844};
RX PubMed=23450133; DOI=10.4056/sigs.3036810;
RA Rawat S.R., Mannisto M.K., Starovoytov V., Goodwin L., Nolan M., Hauser L.,
RA Land M., Davenport K.W., Woyke T., Haggblom M.M.;
RT "Complete genome sequence of Terriglobus saanensis type strain SP1PR4(T),
RT an Acidobacteria from tundra soil.";
RL Stand. Genomic Sci. 7:59-69(2012).
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 -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
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DR EMBL; CP002467; ADV81538.1; -; Genomic_DNA.
DR AlphaFoldDB; E8V5K4; -.
DR STRING; 401053.AciPR4_0705; -.
DR KEGG; tsa:AciPR4_0705; -.
DR eggNOG; COG5009; Bacteria.
DR HOGENOM; CLU_006354_2_7_0; -.
DR Proteomes; UP000006844; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004180; F:carboxypeptidase activity; 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: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; 2.
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 PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF11; PENICILLIN-BINDING PROTEIN 1B; 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 Glycosyltransferase {ECO:0000313|EMBL:ADV81538.1};
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 Reference proteome {ECO:0000313|Proteomes:UP000006844};
KW Transferase {ECO:0000313|EMBL:ADV81538.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 38..60
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 91..260
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 447..685
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 745..823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..770
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..823
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 823 AA; 89962 MW; 14A3893B2BA8E61A CRC64;
MQSPFDRDDS GRNLLLEEQG GARFRVPKFA NRKVARRSAF YVMLGASAIF GGLVGLMLIY
STELPQMADL ERYRPNTTTQ LLDVHGRSFG SFALERRVVV PYSEFPPMLR DAILSIEDKS
FEKNAGVNPI RLVEAAYLDM HSHGRGQGAS TLTMQLARNL FLSAEKTYKR KILEIFLTIQ
IERHFTKDQI FALYANQIYL GHGTYGFEAG SEFYFSKHVH DLTLPEAALL AALPKGPESY
SPIRHPQRAL KRRNLVLSEM LSDKQISVAQ YEVARQSPLG LHIETPANSV APYFVEEVRR
QLEQQYGAEQ VHGAGLKIYT TMDLDLQMTA YKAVMSGVAT YERRHGWKAH LQNIAEAGVD
LETYKHPDWT GPLAEGTYVH ALVTDVTPKK VTLRIGNHMV ELAPEDWAWT KFKSAAEFLT
RGDIAYVRVL ADTDKVALEQ DSGAQASLMA VDNSNGEVLA MVGGRDFALS QFNRATQAER
QVGSSFKPYV YTAAVEAGAK PSDIIVDGPT SFYTPNGPYT PHNYEADYKG AMTLLNAFAE
SRNIPALKLA NQVGIRKVIE VAHRFGVTSN IPSFLPVAIG SAGISLVEQV GSYSVFPNDG
IRVEPHYIRK VVQADGLPLQ QNAPQVKEVI SVETARTMMK FLEAVPQYGT AAQAGAILKH
PLGGKTGTTN DYTDAWFIGF SPSVTCGTWI GYDDRKSLGE KETGAKAALP MWIDFMKVAI
ARTPNEAFPT ANAPKKALQL LAPDANAEPA KPKADADDDA DDDAETKKAA PVERVAPPTS
VPADESAPAG PKPVAKPIVI PPNAPVTKPA PANGPKPVVI PPS
//
