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
//