ID A0A1F5DV62_9BACT Unreviewed; 859 AA.
AC A0A1F5DV62;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=A3I57_00655 {ECO:0000313|EMBL:OGD58974.1};
OS Candidatus Beckwithbacteria bacterium RIFCSPLOWO2_02_FULL_47_23.
OC Bacteria; Candidatus Beckwithbacteria.
OX NCBI_TaxID=1797463 {ECO:0000313|EMBL:OGD58974.1, ECO:0000313|Proteomes:UP000176364};
RN [1] {ECO:0000313|EMBL:OGD58974.1, ECO:0000313|Proteomes:UP000176364}
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:OGD58974.1}.
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DR EMBL; MEZQ01000042; OGD58974.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5DV62; -.
DR Proteomes; UP000176364; 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 NCBIfam; TIGR02074; PBP_1a_fam; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF33; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; 1.
DR Pfam; PF17957; Big_7; 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 26..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 85..253
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 344..628
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 859 AA; 95490 MW; 94F7D11039DF8630 CRC64;
MANWQRIWRQ RLFKMRQFRV RSKADLIRLL AVLAFFGLIF GFLVTTVLFA WYSKDLPRPD
KVVRREGFAT KIFDRNSELL YDVFADQRRT PVTLDQIPQD LREATIAIED KNFYKHEGFD
PLGVVRAMFN TVFRFRRLAG GSTLTQQLVK NVLLTPERAV SRKIKEFVLS VQIEKKYTKD
QILQMYLNES PYGGTAWGVE AAAETYFGKP VSELNLIESA VLAGLPQSPT QYSPFGQNPE
AYKQRTKDVL RRMREDGYLT KDEEKQSLEQ LNQVNFSDTG GEFKAPHFVM YVRQQLIERY
GEKLVEQGGL KVTTTLDWKL QEEAQKIVAE EIARVEDLHI TNGAGLVLDT KTGEILAMVG
SKNYFAPDYE GKVNVNLSLR QPGSAIKPVT YVTAFEQGMT PAKMIVDVAT EFPGGANLPV
YKPKNYDGKD HGPVQLRLAL GNSLNIPSVK LLQLVGVKNM LETAYKLGLT TLEPTNENVN
RFGLSVTLGG GEVKLIDMVT AYSSFGNGGL KIEPISILKV EDQSGKVLEE FRPVAGPRVL
SEAEAFLISD ILSDNSARLI TFGANSLLKI PGSQVAVKTG TTDDQRDNWA VGWTPDRIVG
IWVGNNDNSQ MKQVASGVSG ATPIWRRIIL EALKGQPIKG WPVPSGVASV SVDAISGLVS
HDGWSSRSEY MIKGTEPVGV DTIHTKLKLC RGQNKLASDP MVARGDYEEK EFIVLKEDDP
AGGGKNRYQE GIDAWIAKQS DERYRFPTEF CGESNEVVVQ IESPADKAKI GNDFTFKAKV
TGNKTIKKVI FYADGVEKKT FTGKPYEYTQ HLDNGTHTLK VRGEDELGNA GESEIKIGVG
VNWDWVEASP SATPLPSPS
//
