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Database: UniProt
Entry: A0A1F6MW42_9BACT
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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
//
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