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
//