ID A0A1F6MW42_9BACT Unreviewed; 944 AA.
AC A0A1F6MW42;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=A3G00_04070 {ECO:0000313|EMBL:OGH75643.1};
OS Candidatus Magasanikbacteria bacterium RIFCSPLOWO2_12_FULL_43_12.
OC Bacteria; Candidatus Magasanikbacteria.
OX NCBI_TaxID=1798692 {ECO:0000313|EMBL:OGH75643.1, ECO:0000313|Proteomes:UP000178347};
RN [1] {ECO:0000313|EMBL:OGH75643.1, ECO:0000313|Proteomes:UP000178347}
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:OGH75643.1}.
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DR EMBL; MFQN01000004; OGH75643.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6MW42; -.
DR STRING; 1798692.A3G00_04070; -.
DR Proteomes; UP000178347; 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; 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 33..55
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 84..255
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 344..623
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 944 AA; 105145 MW; 1210E3EAF2753AC8 CRC64;
MSSGDNRRRV YGYTTKNHHS VIRKAGGRFW RKLGWLALVG LVFVFLIGTI MVAWASRDLP
DPDKLTDRKV AQSTKILDRT GEHLLYEVYA QEKRTLVELD QVPQFLINGV IATEDTEFFQ
HKGIRPLSIL RAVVYGVFTN KRIGGTSTLT QQLVKNAVLT NERKITRKIK EIILSIRLEQ
KYTKEQILKI YFNEIPYGST NYGVESAAQS YFGKHVSDVT LAEAATLAGL PKAPSLYLND
PDKLKNRRDF VLERMVAEDY ISREEADAAQ AEPLKIKQKI ENIQAPHFTL YVKGQLVDMF
GEQLVDTGGL KVITSLDWEK QQAAELAIKE NEKSLLEAGA NNAALMAMDP KNGQILSMIG
SRDFFDETID GQFNVATLGK RQPGSSFKPI IYAAAFEKGY TPDTVLFDVL TNFAVSGKPY
QPVDYDSKER GPVSMRQALQ GSLNIPAVQT MYLVGQDKSV EFAKKMGYTT LSDGEFGLTL
VLGGGEIKLL DHVRAYSVFA ANGNKFEPVS ILRVEDSVGG TLFEWKKTKG EKVLDEKITA
TISNVLSDDA SRAYMFGAGG TLTLPNRSVA AKTGTTNNYV DAWTIGYTPS FVAGVWAGNT
DNTQMKQGYG GSKVAGVIWN KFMREALKNA PVEAFPEAPP NDAEKPILRG STGGAITLSI
DKLTGKLASS STPEKYIIQR SYLPAHSILH YVNKDDPRGP ALENPADDPQ YQIWENAIQD
WIKRTKEKNP DWQISFEDPP TEYDDTHSSE LAPTIEIIYP TDGAVLYSRQ IDTNFRFGAP
RGVTRVSYKI DARYVGVIKA PPFNLNYYAK WLESGAHTLI ILAEDDIGNK TEQTINFTLQ
AGEEPPSVSW VEKNKTVSQN NFPIRLALEP FKLEQIKEIL IYQQKSGEEK TILTTITDFS
NLFNNQILFT WSSAPETGVW TLIAEVKPKN GGQTKSEVVE ILVK
//