ID A0A1F6DFJ1_9BACT Unreviewed; 737 AA.
AC A0A1F6DFJ1;
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=A3C89_02315 {ECO:0000313|EMBL:OGG60199.1};
OS Candidatus Kaiserbacteria bacterium RIFCSPHIGHO2_02_FULL_50_50.
OC Bacteria; Candidatus Kaiserbacteria.
OX NCBI_TaxID=1798492 {ECO:0000313|EMBL:OGG60199.1, ECO:0000313|Proteomes:UP000178794};
RN [1] {ECO:0000313|EMBL:OGG60199.1, ECO:0000313|Proteomes:UP000178794}
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:OGG60199.1}.
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DR EMBL; MFLF01000009; OGG60199.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6DFJ1; -.
DR STRING; 1798492.A3C89_02315; -.
DR Proteomes; UP000178794; 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 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..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 66..250
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 340..605
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 737 AA; 81833 MW; 97704A1D972FE06C CRC64;
MKKKSPSRMR RIASDIVLFG TVFFLVAIGS LFVWVATLDI PDLSAFNQRL VAQSTKLYDR
TGETILYDTN SDVRRTVVRY DEISEYLKNA TIAIEDAEFW THAGVRPTAI VRSMITSLSQ
GKGVFSGGGG STITQQVIKN SVLQQERSLT RKIKEAILAI RLEQVMEKDE ILLTYLNESP
YGGTLYGVEE AAQAFFGKHA NEVTLAEAAY LASLPQAPTR LSPYTQSFRD PQTREVSQLE
VRKNYVLTRM EEEGMITKDE AEIARAEEVA WKPYISATIR APHYVMYVLE QLQEKYGDEY
LNKGYKIITA VDLPLQEKAE AIVKEYALKN DAAYNAANAS LVAEDPKNGD VLVLVGSRDF
FEENIDDPRV AGQYNVATNE TPGRQPGSSF KPFIYATAFE KGYTPDSILF DVETQFSTAC
AVDNFKTNSE DPNCYSPKNY DHQFRGPVSI RNALAQSLNV PAVKMFYLAG RKSSVKTARD
MGITTLPDTT PSLDLVLGSG EVTLYQMVSA YAVFASEGIK IEPRTVLRIE DSRSTVLKEF
DEVNAGRVLE RNTALNISSI LSDNAARAPL FGANSPLHFG ERDVAAKTGT TNDKKDVWII
GYTPNLVAGA WAGNNNNVEM KEISGLIITP LWRAFMDEAL RELPSESFPE PTHTVTGKPI
LDGVWLGMNT YGEPEIHSEL YFIDSENPTG SQPNNPNSDP QFKYWEYGVL NWLQGLLGQN
NTSFPSLSTT TTEVIGQ
//
