ID A0A1V2YJ80_9FIRM Unreviewed; 383 AA.
AC A0A1V2YJ80;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Probable peptidoglycan glycosyltransferase FtsW {ECO:0000256|ARBA:ARBA00041185};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
DE AltName: Full=Cell division protein FtsW {ECO:0000256|ARBA:ARBA00041418};
DE AltName: Full=Cell wall polymerase {ECO:0000256|ARBA:ARBA00033270};
DE AltName: Full=Peptidoglycan polymerase {ECO:0000256|ARBA:ARBA00032370};
GN ORFNames=BEN18_03695 {ECO:0000313|EMBL:OOB79611.1};
OS Epulopiscium sp. Nuni2H_MBin001.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Candidatus Epulonipiscium.
OX NCBI_TaxID=1884656 {ECO:0000313|EMBL:OOB79611.1, ECO:0000313|Proteomes:UP000189057};
RN [1] {ECO:0000313|Proteomes:UP000189057}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL Submitted (JUL-2016) 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 -!- SIMILARITY: Belongs to the SEDS family. FtsW subfamily.
CC {ECO:0000256|ARBA:ARBA00038053}.
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:OOB79611.1}.
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DR EMBL; MDJM01000008; OOB79611.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V2YJ80; -.
DR STRING; 1884656.BEN18_03695; -.
DR Proteomes; UP000189057; 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:InterPro.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; 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 3: Inferred from homology;
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:UP000189057};
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 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 52..69
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 76..99
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 119..136
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 143..159
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 165..181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 188..210
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 283..309
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 321..340
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 360..379
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 383 AA; 41789 MW; BEC700400562A69A CRC64;
MIKVREDNKL DIALVGIILA ITIFGVLMVY SASNYYALVT SNDPFNLVKR QGIYASLGVM
LMFIIAYCVD YKVFSNIIIS VTIYILANLS VVALLFIGYE SNGATRWIRI GSFSFQPSEL
AKVATILLLS TVIERYRSKL DDVRFLILCL VIILIPGVLV LREDMSSAIV IVAASLLILF
VSTPQIWYYV AGVIVGIVGI FYTLFLAATI DPNVQITGIL GMILPQYRLN RFRVWLDPWT
DPYGFGYQPI QSLYAIGSGG LFGQGFGMSI QKQGFLPEPH NDIIFSVICE ELGLVGASVV
LIAYSIFVFK GFLVALNAKD LFGSLVASGL VGLVAIQVII NVGVNTNLFP TTGMQLPLIS
YGGTAIIVLL ASLGILLNIS KHV
//
