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Database: UniProt
Entry: A0A1G2JD31_9BACT
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ID   A0A1G2JD31_9BACT        Unreviewed;       736 AA.
AC   A0A1G2JD31;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-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=A2401_02785 {ECO:0000313|EMBL:OGZ84330.1};
OS   Candidatus Staskawiczbacteria bacterium RIFOXYC1_FULL_38_18.
OC   Bacteria; Candidatus Staskawiczbacteria.
OX   NCBI_TaxID=1802229 {ECO:0000313|EMBL:OGZ84330.1, ECO:0000313|Proteomes:UP000177751};
RN   [1] {ECO:0000313|EMBL:OGZ84330.1, ECO:0000313|Proteomes:UP000177751}
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:OGZ84330.1}.
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DR   EMBL; MHPP01000019; OGZ84330.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G2JD31; -.
DR   STRING; 1802229.A2401_02785; -.
DR   Proteomes; UP000177751; 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   NCBIfam; TIGR02074; PBP_1a_fam; 1.
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   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        23..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          77..246
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          334..639
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   736 AA;  82205 MW;  E22B6EFC62902753 CRC64;
     MAKKNFPLKN LKEFLARHNI KKYLAYFCLT GFLFFVLLFF YYTWDLPKPE KFTETPFIQS
     TKIYDRTGRV VLYDIFGEEK RQIVPFNKIS DHLKQAVLTS EDARFYQHGG IDFEGILRAV
     WVDLLSQARS QGGSTITQQL IRTVYLTGQK SISRKIREIV LSIELEQKYS KDQIFEWYLN
     AIPFGENAYG AESASQTYFS KPASDLSLAQ AATLTSLIPA PSHYSPYGPN KAELLQKKDS
     VLERMKKNGY ITTEEMEEAK KEKIVFSETT NSIKAPDFVL YIKKYLDDKY GEDYLRERGL
     RIYSTLDWDL QQYMEKTIKE SDKSLKSKNA NNAAAAAINP KTGEILALVG SKDYFAKPYP
     EGCDEKGPNA CLFAPKYDVA TMGKRQPGSS FKPIVYATAF KKGFTPNTIL WDVNTEFNPN
     CPPDGTGITD QYGLKCYSPQ DYDGGNRGPV TMRQALDQSL NIPAVETLYL TGIYDSLQTA
     RDLGITTLTD INNYGLSLVL GGGDVNLLEM TSAYGVFAAE GIYIPPISIL KITDSDGNII
     EENKKQPTKV LDTQIARTVN NVLSDNNARA PIFGFNSPLY FPNYQVAAKT GTTQNFVDGW
     TMGYAPSIAV GVWVGNNNNV PTRDEGIGLA APIWHKIMEK VLLSQPAENF NPPEPITTGR
     NPALLGQLPT GDTNTILYYV DKNNPLGSSP QNPASDPQYF MWQAAINNWL SKNNTALNSI
     DTASNSTNKT VDVKLP
//
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