ID A0A023AWJ4_GRENI Unreviewed; 179 AA.
AC A0A023AWJ4;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
DE AltName: Full=Peptidoglycan polymerase {ECO:0000256|ARBA:ARBA00032370};
DE Flags: Fragment;
GN ORFNames=GNI_243520 {ECO:0000313|EMBL:EZG42615.1};
OS Gregarina niphandrodes (Septate eugregarine).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Gregarinasina;
OC Eugregarinorida; Gregarinidae; Gregarina.
OX NCBI_TaxID=110365 {ECO:0000313|EMBL:EZG42615.1, ECO:0000313|Proteomes:UP000019763};
RN [1] {ECO:0000313|EMBL:EZG42615.1, ECO:0000313|Proteomes:UP000019763}
RP NUCLEOTIDE SEQUENCE.
RA Omoto C.K., Sibley D., Venepally P., Hadjithomas M., Karamycheva S.,
RA Brunk B., Roos D., Caler E., Lorenzi H.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:EZG42615.1}.
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DR EMBL; AFNH02001968; EZG42615.1; -; Genomic_DNA.
DR RefSeq; XP_011134798.1; XM_011136496.1.
DR AlphaFoldDB; A0A023AWJ4; -.
DR EnsemblProtists; EZG42615; EZG42615; GNI_243520.
DR GeneID; 22916864; -.
DR VEuPathDB; CryptoDB:GNI_243520; -.
DR Proteomes; UP000019763; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR InterPro; IPR001182; FtsW/RodA.
DR PANTHER; PTHR30474; CELL CYCLE PROTEIN; 1.
DR PANTHER; PTHR30474:SF2; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE FTSW-RELATED; 1.
DR Pfam; PF01098; FTSW_RODA_SPOVE; 1.
PE 4: Predicted;
KW Cell cycle {ECO:0000313|EMBL:EZG42615.1};
KW Cell division {ECO:0000313|EMBL:EZG42615.1};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Reference proteome {ECO:0000313|Proteomes:UP000019763};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 140..161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EZG42615.1"
FT NON_TER 179
FT /evidence="ECO:0000313|EMBL:EZG42615.1"
SQ SEQUENCE 179 AA; 19805 MW; DD30108ED121B59D CRC64;
FFSPVVLVAG IILLVFIQPD LGGASILAAV MVVMFFGTGM SYWYGFSLIT AVTTTVMILF
SILRHFNFST NVNSYKFNRI LSFLHPFELE NMGGSQLVNS YYAINNGGWF GLGLGNSIQK
RGYLPEPYTD FILSITTEEL GVIGTLVIIA LLFALLARIF YLGIHATKMY HTLLCYGIG
//
