ID A0A0S7X537_9BACT Unreviewed; 653 AA.
AC A0A0S7X537;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=AMJ49_00375 {ECO:0000313|EMBL:KPJ57566.1};
OS Parcubacteria bacterium DG_74_2.
OC Bacteria; Candidatus Parcubacteria.
OX NCBI_TaxID=1703766 {ECO:0000313|EMBL:KPJ57566.1, ECO:0000313|Proteomes:UP000051668};
RN [1] {ECO:0000313|EMBL:KPJ57566.1, ECO:0000313|Proteomes:UP000051668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG_74_2 {ECO:0000313|EMBL:KPJ57566.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPJ57566.1}.
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DR EMBL; LJNF01000001; KPJ57566.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S7X537; -.
DR PATRIC; fig|1703766.3.peg.746; -.
DR Proteomes; UP000051668; Unassembled WGS sequence.
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; 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 PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF33; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; 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 Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 74..247
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 336..640
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 653 AA; 74138 MW; A9A0E7338AF93CFF CRC64;
MVKRSFSRNI LKKREAKRKL FLKVFGFLFL FFLFFVSVVF IYYAKDFPRP EKFGERELFQ
STKIYDRTGE ILLYEIYGEE KRTLVSLDKI PEYLKNAVIV AEDANFYHHF GIDLKGIARA
ILVDLRIKKP VYGGSTIPQQ LIRSTFLSLE KTAQRKIREI ILALELDRRY SKDQILEWYL
NQVPFGQNAY GVEAASQTYF KKSVSEVSLA ESAVLASLIR APYRLSPYDE EGKKELLIRK
DYVLERMVEE GYLTSEEAEK EKKEEIEFAE KKVEILAPHF TLQVKNQLEE IYGRRFLEEK
GLKVFTTLDW ELQKWAEEVV SIGTERNKIY GAYNTSLVAL DPKNGEILVM IGAAIKSGDY
PGKPYPENCQ PGKDCLFDPE FNVAIGEPGR QPGSAFKPFV YATAFKKGYD DETVVVDEPT
NFGVWGGKEY IPQNYDGKFR GPVTLRGALA QSINVPSVKV LLSLADSPED FKENREPDSI
KTAKDLGITT LNPPYGPSIV LGGWEVKLLE MTSAYGIFAT NGMKVSPLSI LKIEDANGNL
IFSNQKKSKR VLPSETCKLI NDILSDNEAR SPMFGQRSSL YFEGYEVAVK TGTTQNYKDA
WTIGYTPFIS VGVWVGNNDG TPIKKPGVTA AAPIFHQFLE RVLLEYPKEN FED
//
