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Database: UniProt
Entry: W9AQG0_9BACI
LinkDB: W9AQG0_9BACI
Original site: W9AQG0_9BACI 
ID   W9AQG0_9BACI            Unreviewed;       675 AA.
AC   W9AQG0;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   Name=pbpG {ECO:0000313|EMBL:CDO05097.1};
GN   ORFNames=BN988_03679 {ECO:0000313|EMBL:CDO05097.1};
OS   Oceanobacillus picturae.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=171693 {ECO:0000313|EMBL:CDO05097.1, ECO:0000313|Proteomes:UP000028863};
RN   [1] {ECO:0000313|EMBL:CDO05097.1, ECO:0000313|Proteomes:UP000028863}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S1 {ECO:0000313|EMBL:CDO05097.1,
RC   ECO:0000313|Proteomes:UP000028863};
RA   Croce O., Lagier J.C., Raoult D.;
RT   "Draft genome sequencing of Oceanobacillus picturae strain S1 isolated from
RT   human gut.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDO05097.1, ECO:0000313|Proteomes:UP000028863}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S1 {ECO:0000313|EMBL:CDO05097.1,
RC   ECO:0000313|Proteomes:UP000028863};
RA   Urmite Genomes U.;
RL   Submitted (MAR-2014) 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   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752}.
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:CDO05097.1}.
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DR   EMBL; CCAX010000004; CDO05097.1; -; Genomic_DNA.
DR   RefSeq; WP_036578535.1; NZ_CCAX010000004.1.
DR   AlphaFoldDB; W9AQG0; -.
DR   STRING; 171693.BN988_03679; -.
DR   eggNOG; COG0744; Bacteria.
DR   Proteomes; UP000028863; Unassembled WGS sequence.
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   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   Membrane {ECO:0000256|SAM:Phobius};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028863};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          57..231
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          322..565
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   675 AA;  75374 MW;  5DEF74D4CA90AA24 CRC64;
     MGKGKYNLGS KLLLKLIVWL VAVILLGAGA IYLTSFLLGP PDLQMDQNTI LYSTNEEVIG
     EERGPEYRQW VELSDMSEEI IAATLLTEDQ NFYNHHGFDL KRIMGAIVKD IKTWSLKEGA
     STLTQQYARN LYLTHEKSLT RKIKEAFYTV RLEMFYSKED ILEGYLNSIY YGHGAYGIEA
     ASNYFFNKSA TDLTVAEAAM LAGIPKGPTY YSPLNDEERA RNRQKQILTN LLDKGIIDQK
     SFDSALRQEL IYAKNSPNSQ EKIAPHFQDT VIKEAAELLG RKQKEVRSGG YSIYTTLNTK
     QQKLLEQQVE KTAQPETELE IGALALDPST GGITAMLGGR DYNQSPFNRT TSAKRMPGSS
     FKPFLYYAAL ENGYTPNTML MSKPTSFELA DGNVYQPSNF NGYYANEPIT LAQAIALSDN
     VYAVKTNMYL GPERLVDAAK EFGITSKLPA VPSLALGTAT VNVKEMVTAY GMLANGGHEL
     QGHTIEKIVD REGKTVYKHK TKEGKQKLDQ KTAFLLTQLM TGMFDRELDG YMSVTGSSVS
     DQLSRIYAGK SGTTNSDSWM IGYSPSLVTG IWAGYDDNRP MEKVAESAYT KQIWAGFMEA
     AHEDIPIENF TAPSGVVGIP IDPVTGLRAT PYCESSRVMY FEKGTEPEGY CTEHYHQEDK
     DEEKSMVEQL FDLFR
//
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