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Database: UniProt
Entry: A0A1G3QH65_9SPIR
LinkDB: A0A1G3QH65_9SPIR
Original site: A0A1G3QH65_9SPIR 
ID   A0A1G3QH65_9SPIR        Unreviewed;       916 AA.
AC   A0A1G3QH65;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=A2176_09780 {ECO:0000313|EMBL:OHD66041.1};
OS   Spirochaetes bacterium RBG_13_51_14.
OC   Bacteria; Spirochaetota.
OX   NCBI_TaxID=1802193 {ECO:0000313|EMBL:OHD66041.1, ECO:0000313|Proteomes:UP000176595};
RN   [1] {ECO:0000313|EMBL:OHD66041.1, ECO:0000313|Proteomes:UP000176595}
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:OHD66041.1}.
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DR   EMBL; MIBH01000017; OHD66041.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G3QH65; -.
DR   STRING; 1802193.A2176_09780; -.
DR   Proteomes; UP000176595; 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; 2.
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   NCBIfam; TIGR02074; PBP_1a_fam; 1.
DR   PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR32282:SF27; PENICILLIN-BINDING PROTEIN 1A; 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        121..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          164..337
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          522..812
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   916 AA;  102541 MW;  0F7713571C84E00A CRC64;
     MAKYQGKPTR FSRDGIIKSA GDHVASSDRT RKAVAALIDR LRNAAGMVGN PLRSVLSRIR
     DRIPLNTVIQ KASDYRSQRL AGSQRYAMSA YSLPGALERI VSRCVEITRS LFFAVRRSRT
     AVIGIIAGAM IAFGVILAMD FVRVKSLATF QPNATTKIYD RHGMLVSEIF AQKRDVVPLK
     KIPRDLANAF IAIEDNEYYD HWGVNPKGIV RAFFINIFSG RIRQGGSTIT QQLAKVLLTS
     QERNIFRKIK EAFIAVMMEM TYSKDEILSL YLNQIFLGHG TYGVEAASKL YFDKHVWQLN
     LAECSLLATL PSAPNQFSPI RHPKRSIQRH KIVLAKMVET GFISVKQAEQ AFLDFWPDYL
     DYVSELAPTM TTMSARENKA PWVTEYVRRE LVRKYGYEMV YEKGLQVHTT LDLKKQLAAQ
     DVLKRILERQ SETSAKLSFK NEDYIVDNYG DAVELFRLLF DIPAFRKKGS RQREKINNFI
     RDEIVEELDG LNYLAGIDSV SSFLDRYKGT YLEDKNLQKV EGCVVSIDHR NGYIEAMVGG
     SEFTSINQLN RVQQARRQPG SAVKPLIYAA AIESGEFTAA SSVMDSPVVF LESDGGDWIP
     ENYEGEYSGF VRLRKALALS INVVSIRISQ QLGIEYVMKY LSKLLKFDKA ETKERIPRNF
     SIALGSMEVS PLELTTAYGI IANGGRDVIP YAIRYVKDRM GNVLENREEE VQKILADEER
     DGTLQILKPE TAQVLISMMQ SVISGGTGGS ASPGRPAAGK TGTTNNWKDA WFVGFTPQVT
     TGVWVGYDKM GLSLGIGQSG GAVAAPIWGE YMREGLKDEP VLDFPQYGGL ITHEVCELSG
     LLPSADCRDT IEEIFVPGTV PSKTCDMCAD IIGGVNLPKK GPAEDITKEQ KKTIIRQMEK
     KKHESIFEHI HDDLLK
//
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