ID A0A1F6A0X3_9BACT Unreviewed; 731 AA.
AC A0A1F6A0X3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=A3D78_07395 {ECO:0000313|EMBL:OGG17947.1};
OS Candidatus Gottesmanbacteria bacterium RIFCSPHIGHO2_02_FULL_39_14.
OC Bacteria; Candidatus Gottesmanbacteria.
OX NCBI_TaxID=1798383 {ECO:0000313|EMBL:OGG17947.1, ECO:0000313|Proteomes:UP000176253};
RN [1] {ECO:0000313|EMBL:OGG17947.1, ECO:0000313|Proteomes:UP000176253}
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:OGG17947.1}.
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DR EMBL; MFJM01000026; OGG17947.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6A0X3; -.
DR STRING; 1798383.A3D78_07395; -.
DR Proteomes; UP000176253; 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 7..23
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 29..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 78..101
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 135..308
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 396..679
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 731 AA; 82525 MW; A375B5F6EA31C381 CRC64;
MSRFGNFIIS LLIIPLYIFK QIGELIIETI IYIISAIFST YKLFILSFYE FLKLPYRLLR
FLIVKSRRKK RNKLRKKLSL AVIKTKYFLL GIFFLGMIIS FQQLHSFVIN LPNPRQINLA
GFPVTSKIYD RDGILLYEIY ERFNRTPIKL NQVPKYVIEA TIATEDEEFY LHNGISLRGI
SRALIHNLTS DSLEGGSTIT QQLIRSTYLT PEKTLIRKLK EIILSIWIEA IYSKNQILEM
YLNQVPYGGT AWGIEAAAKT YFNKKTSELN LAEAAFLAGL PAAPTKYQPF GNPEKIYKKR
QEEVLKRMLK ESFINNKEYS EAIAFPLNIT EPRIPIAAPH FVMYTKELLN KYYGPRLIEQ
GGLRIYTTLD LILQEEVQKI VYEAVEQLKE LKVANGAALV TNPINGEILA MVGSADYYDR
ENDGNVNVTQ SRRQPGSAIK VVNYATALQN GFTAATIIND SPVSFHIAGQ PEYRPVNYDG
KFHGRVTMRT ALGSSYNVPA VKVLNSYGVD RMIETGKKMG IDSWDEKGRF GLSLTLGGGE
VTMMDMAEVY GTLAYGGIRQ NLTPLVKITD YNGKNIPIPK MGKIIRAIPE TVAFILTSIL
TDNDARTPAF GSNSLLNIPG KWVAVKTGTS DNKRDNWTIG YTTDYVVTVW VGNNDNSPMN
PSLTSGITGA APIWREIMEI FLKDKDSQPF IKPDGIITVK CNNKDEYFIE GTFTGRECPN
LTPEQKVQTE N
//
