ID A0A1F7JP31_9BACT Unreviewed; 848 AA.
AC A0A1F7JP31;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=A3J15_01525 {ECO:0000313|EMBL:OGK57389.1};
OS Candidatus Roizmanbacteria bacterium RIFCSPLOWO2_02_FULL_38_10.
OC Bacteria; Candidatus Roizmanbacteria.
OX NCBI_TaxID=1802074 {ECO:0000313|EMBL:OGK57389.1, ECO:0000313|Proteomes:UP000176376};
RN [1] {ECO:0000313|EMBL:OGK57389.1, ECO:0000313|Proteomes:UP000176376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGK57389.1}.
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DR EMBL; MGAY01000004; OGK57389.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F7JP31; -.
DR STRING; 1802074.A3J15_01525; -.
DR Proteomes; UP000176376; 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 Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR001264; Glyco_trans_51.
DR InterPro; IPR013783; Ig-like_fold.
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..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 73..248
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 336..601
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 848 AA; 95064 MW; E85BCEA262C16180 CRC64;
MNVSHVIKYR SYRRRFARGV SMISVTKLFF FGLLFFIAFI FLLFLWYSKD LPEPGKIKRS
SGYSTVIYDR NDKVIFEMYK DENRIPVKLS EMSPFLKKAT ISIEDKDFYR HSGFSLRGYL
RAILSSLIKR RVEGGSTLTQ QLVKTVLLSS ERTFTRKIKE FVLASEIERR YSKDEILEMY
LNEIPYGGTF VGIESAAKGY FGKSARELSL IESAILAGLP QRPSHYSPFI GKPDAYIDRA
LSVLRRMKED KVISLSEYSK AREELKQIKF EHVYSSINAP HFVFYVVEQV SELFGKDIMD
RGIKIKTTID LDLQKKNENI VKTEIEKIKK YDATNGAVVV IDNETGEIIS MVGSYDYNDK
EFGSYNTATA FRQPGSAIKP ITYATAFEKG YTASTVLMDV KTTFPNQGGK DYEPVNYDGL
YHGPIQLRFA LGNSINIPAV KLLAMVGVRN FLQKAYDFGL TGFEPTPANL KRFGLAITLG
GGETTLLNLT SAYATIARGG IRRDYQSILE VTDYKNHKLY ESKKSTDRQV ISRDVAFLLS
HILSDNNARS ATFGTRSYLN IPGKTVAVKT GTTNDLRDNW TIGYTKAVSV GVWVGNNDNS
PMNSKIASGV TGASPIWNQV MSLLLKDRSD GIIDKPDQVI AQEVDASFGG LPYLGSPTRS
EYFIDGTQPK EPSPYYKRLK ISKSSGKLAN EIEIRLGDYD EKDFIVIEEA DPVSTDGVNR
WQKAIDEWSL AQPDGKYHAP RESSTAKADE ISVQIKDPQD KSRTGNNLTL KARIASIDPV
TKIEIFVNGS IIKTLTEDKK EIEENLTLSD GIYELRVRAE NSKGKAGDSI VKIGVNTDWT
AITPTVSP
//
