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Database: UniProt
Entry: A0A1F6DVH0_9BACT
LinkDB: A0A1F6DVH0_9BACT
Original site: A0A1F6DVH0_9BACT 
ID   A0A1F6DVH0_9BACT        Unreviewed;       711 AA.
AC   A0A1F6DVH0;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=A3C94_02130 {ECO:0000313|EMBL:OGG65022.1};
OS   Candidatus Kaiserbacteria bacterium RIFCSPHIGHO2_02_FULL_55_17.
OC   Bacteria; Candidatus Kaiserbacteria.
OX   NCBI_TaxID=1798496 {ECO:0000313|EMBL:OGG65022.1, ECO:0000313|Proteomes:UP000177232};
RN   [1] {ECO:0000313|EMBL:OGG65022.1, ECO:0000313|Proteomes:UP000177232}
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:OGG65022.1}.
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DR   EMBL; MFLJ01000003; OGG65022.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F6DVH0; -.
DR   STRING; 1798496.A3C94_02130; -.
DR   Proteomes; UP000177232; Unassembled WGS sequence.
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: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   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Protease {ECO:0000256|ARBA:ARBA00022670}.
FT   DOMAIN          56..228
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          318..573
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   711 AA;  77066 MW;  8A45FC1267514BC0 CRC64;
     MFLAFILALF GLGFFIGGGL LVVVALTPVP DISSFSSRQV DQSTKIYDRT GQVLLYDYNR
     DARRSVVPLA DISPHAISAT IAIEDSSFYA HGGIRLTSIL RAILADAVGG SLSQGGSTIT
     QQVVKNELLT SRKSIIRKIH EWVLAIKLEQ VYSKEQILET YLNSIPYGGT LYGIEAASES
     YFGIPAKDLS LAQAAYLASM IQAPTYYSPY GTHRAALDAR KDTILERMRT LGFISDAASV
     TAKEEGVSFS PTGRNSIAAP HFVFYILNLL EERYGSQALI SGLKVTTTLD ADLETKAEAI
     VNQYALENEK KFKASNASLI ALDPSTGQIL AMVGSRSFFD TTIDGQYNAS LASRQPGSTM
     KPFIYSLALM KGYTRNTVVF DTPTQFSTAC NPSDIYNNTP PCYAPSDYDN TFRGPMTFET
     ALAQSINIPA LKVLYLVGIQ QAITLAKSFG LTTLGDPNQY GLTLVLGGGE VRLLDLVGAY
     AVFANEGVKN TPTGILEVAD AQGTLLESYA PQSSQVVPAN IARDMSAMLS DAPARLPEYP
     LNSPLSFSGY EVAVKTGTTD DTRDAWVIGY TPSLALGVWA GNNDNSPMVK SIAGFIAAPM
     WHEAMAYALS KYPKTYFGEP SPILSTVPPM LRGDWYIPDA QGNIVPHDLL YWTDKHNPQG
     PPPINPARDP QFAYWEYGLS VWYESHPNLF QGGIMLPVPL STATTSIVMA P
//
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