ID A0A1F6I3Y1_9BACT Unreviewed; 746 AA.
AC A0A1F6I3Y1;
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=A3C22_02025 {ECO:0000313|EMBL:OGH17326.1};
OS Candidatus Levybacteria bacterium RIFCSPHIGHO2_02_FULL_37_10.
OC Bacteria; Candidatus Levybacteria.
OX NCBI_TaxID=1798600 {ECO:0000313|EMBL:OGH17326.1, ECO:0000313|Proteomes:UP000178573};
RN [1] {ECO:0000313|EMBL:OGH17326.1, ECO:0000313|Proteomes:UP000178573}
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:OGH17326.1}.
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DR EMBL; MFNX01000026; OGH17326.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6I3Y1; -.
DR Proteomes; UP000178573; 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 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 104..126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 154..326
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 415..694
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 746 AA; 82935 MW; 6A9114CEB7070159 CRC64;
MNLFQDAAIT IIKILIAIGD VTLLVLSSMA RFLKRITKRI VNSVKLILKF FAQAYKKATY
ILSVLRRFKI KFKKYRVSKP KIKKIKKAKP IKIFPFPFFV KAKYFLIGSL FSAIFIFLPL
LFLIFLQDLP SPKILGLQEN PQTTKIYDRH EVLLYQIYAN QNRTFVPLSS IPKQLQNATI
AIEDKDFYSN PGFNIGAILR ATIANLSGKP LQGGSTITQQ LIKATLLTPE ISMTRKIKEI
ILSFWAERIY TKDQILQMYL NQISYGGTSW GVEAASQTYF GKHAKDLDLA QSAFLAGLPN
APTLYSPYGE FPNLWKKRQK EVLLRMVEQR LITPKEKEDA EREELAFQPI QNSIHAPHFV
MYVKDLLVKK YGLPMVEKGG LQVVTTLDLK TQEGAEKIVK EEVENNRNLN LTNGASLITN
PKNGDIIAMV GSHDYSDPNG GNFNATTALR QPGSSIKVIT YSAALSSSFT AATIIDDSPI
SFTSANAPPY SPVNYDGRFH GLMTLRTALA NSINIPAVKT LNTIGIPTMV ELGKKMGIST
WKEPEDYGLA ITLGAADVKM SDMAVVYGVL ANEGNRVDLN PILKITDYRG NVLEEKKVEK
KRVLSPGVAF IISDILADNK ARAMEFGINS PLLIQNHTVS VKTGTSDNKR DNWTIGFTPS
YLVAVWVGNN NNSPMSQNLA SGITGAAPIW HRVMENLISS KPDEKIPVPE DIVRKPCLGA
NEYFIKGTEN FVNCTPKISP AVSKTP
//
