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Database: UniProt
Entry: A0A1F7XL17_9BACT
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ID   A0A1F7XL17_9BACT        Unreviewed;       824 AA.
AC   A0A1F7XL17;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=A2V97_03110 {ECO:0000313|EMBL:OGM15742.1};
OS   Candidatus Woesebacteria bacterium RBG_16_42_24.
OC   Bacteria; Candidatus Woesebacteria.
OX   NCBI_TaxID=1802485 {ECO:0000313|EMBL:OGM15742.1, ECO:0000313|Proteomes:UP000177382};
RN   [1] {ECO:0000313|EMBL:OGM15742.1, ECO:0000313|Proteomes:UP000177382}
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:OGM15742.1}.
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DR   EMBL; MGFX01000001; OGM15742.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F7XL17; -.
DR   STRING; 1802485.A2V97_03110; -.
DR   Proteomes; UP000177382; 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:SF11; PENICILLIN-BINDING PROTEIN 1B; 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        36..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        123..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          173..346
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          434..691
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   824 AA;  90692 MW;  C5241D67AEA3E259 CRC64;
     MARGARKKPD VFLAPKINFK VLTLTKGLLV GVGKPLFYLL SFAVILVLFI SYHLGGLITS
     LISLFFKSLK RAIKVKAPKL KLKISKVKKP KIPTWPTRLF LLKLRLKLLR IPKIKIPKIR
     IRLGALLLTV LLLPFALAFS FWILFLRDLP SPQELTTREI EVSTKIYDRN GVLLYKIFED
     QNRTIVPLTE IPLQVRLATL AIEDAEFYTH PGFSLKGIFR ALARNISTGE LTGGSTITQQ
     LVKNALLSPE KTFTRKVREV ILSIWVELTY TKDEILEMYL NEVSYGGTAY GIQEASQVYF
     EKDVDELSLG EAALLAGLPK SPTSFSPFGP NPQASLERQR EVLRLMVINK FITTEEAQRA
     IEAGLVFAPN KTDIKAPHFV MFVKQALVDK YGEEVVEKGG LEVTTTLDYD IQRLAEEAIK
     TELEKLGKLN VGNGATLVVS PSTGEVLAMV GSKDYFDTAH DGNVNVVTAP RQPGSSIKVV
     NYSYALSNGF TPATILSDTP VTFSVPGQPP YSPKNYDGAF RGNLPLRNAL AESRNVPAVK
     VLASYGVTKM IEQGVSMGIT TWTDPSRYGL SLTLGGGEVK LIDLAKVYAT VANYGKRPEF
     TAIRRVTNYK GKVLDANCES AKSDGFAEVA AKEAACEWEQ VVDPRVAFIL IDILKDNAAR
     APAFGSSSQL VISGRNDVAV KTGTSNDLRD NLTIGFNQEF LVAVWVGNND NSPMARIASG
     VTGAAPIWNK IMSGVLARTL NHPWEPPSGL VQISVCPLTG TLSCEGCATR TEWFLEETKP
     IKACVLKQED DAKAPQILEP APAIEVIPQP LVTPKPRRWR RLQF
//
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