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Database: UniProt
Entry: G5SW77_9BACT
LinkDB: G5SW77_9BACT
Original site: G5SW77_9BACT 
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
//
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