ID G5SW77_9BACT Unreviewed; 775 AA.
AC G5SW77;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=HMPREF9441_03648 {ECO:0000313|EMBL:EHG98541.1};
OS Paraprevotella clara YIT 11840.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Paraprevotella.
OX NCBI_TaxID=762968 {ECO:0000313|EMBL:EHG98541.1, ECO:0000313|Proteomes:UP000003598};
RN [1] {ECO:0000313|EMBL:EHG98541.1, ECO:0000313|Proteomes:UP000003598}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIT 11840 {ECO:0000313|EMBL:EHG98541.1,
RC ECO:0000313|Proteomes:UP000003598};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (MAR-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:EHG98541.1}.
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DR EMBL; AFFY01000074; EHG98541.1; -; Genomic_DNA.
DR RefSeq; WP_008622856.1; NZ_JH376642.1.
DR AlphaFoldDB; G5SW77; -.
DR STRING; 762968.HMPREF9441_03648; -.
DR GeneID; 78584368; -.
DR PATRIC; fig|762968.3.peg.3205; -.
DR eggNOG; COG5009; Bacteria.
DR HOGENOM; CLU_006354_2_4_10; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000003598; Unassembled WGS sequence.
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 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670}.
FT DOMAIN 57..238
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 452..691
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 775 AA; 88465 MW; AAF29B557F209612 CRC64;
MRKKFVITLW VILFLCISAV SLAFYAIWHG WIGYMPNLYQ LENPVNKYAS QAVSADGKLL
GTWSYSRANR IFVGFDDLSP WLVKALVATE DERFYDHSGI DYRALARAVV KRGLLGQSNA
GGGSTITQQL AKQLYSDVAQ STMERALQKP IEWVIAVKLE RYYTKEEIIT MYLNYFDFLH
NAVGIKTASR TYFNKEPQNL SVCEAATLIG MCKNPSYFNP VRKPERCRER RNVVLDQMVK
AGYLSKADAE LHKLEPIGLR FHRVDHKEGL ATYLRERLRT MLMAKEPNRS DYASWQDQKY
YEDSLAWETD PLYGWCNKNR KKDGTPYNLY TDGLKIYTTI DSRMQQYAEE SVEEHVAGYL
QPIFDKEKRH QTTRPFSNQL STKEVEKIMR RSMEQSERYI KMKKGGATEE DIQKAFNTPQ
KMTVFSYHGE VDTIMTPMDS IRYYKSFLRA GFMCMDTRTG YVKAYVGGPD YRYFQYDMAG
VGRRQVGSTI KPFLYTLAME NGMSPCDLAP NVQQTYIVAG KPWTPRNGSR SRYGEMVTLK
WGLAQSNNWI SAYLMSRLSP SALVRLIHEF GVLNRDIHPS MSLCLGPCEI SVAEMVSSYT
AFANRGIRTA PLFVSRIEDN EGNVVGEFQP RMTEVISEES AYKMIIMLQG VMNGGTGGRM
RFRYNVNADM GGKTGTTNRN SDGWFVCFTP SLSAGCWVGG EDRDIHFNSM TYGQGASSAL
PVCAYFFQKV YKDKDLGYSP DEKFKIPEGF DPCQDTILTE EAPVEEYGGI DEVFE
//