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Database: UniProt
Entry: A0A2G3E397_9FIRM
LinkDB: A0A2G3E397_9FIRM
Original site: A0A2G3E397_9FIRM 
ID   A0A2G3E397_9FIRM        Unreviewed;       369 AA.
AC   A0A2G3E397;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
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=CSX02_05985 {ECO:0000313|EMBL:PHU37747.1};
OS   Agathobacter ruminis.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Agathobacter.
OX   NCBI_TaxID=1712665 {ECO:0000313|EMBL:PHU37747.1, ECO:0000313|Proteomes:UP000224563};
RN   [1] {ECO:0000313|EMBL:PHU37747.1, ECO:0000313|Proteomes:UP000224563}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JK623 {ECO:0000313|EMBL:PHU37747.1,
RC   ECO:0000313|Proteomes:UP000224563};
RA   Sheridan P.O., Walker A.W., Duncan S.H., Scott K.P., Toole P.W.O., Luis P.,
RA   Flint H.J.;
RT   "Resolving the taxonomy of Roseburia spp., Eubacterium rectale and
RT   Agathobacter spp. through phylogenomic analysis.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PHU37747.1, ECO:0000313|Proteomes:UP000224563}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JK623 {ECO:0000313|EMBL:PHU37747.1,
RC   ECO:0000313|Proteomes:UP000224563};
RA   Banno H., Chua N.-H.;
RL   Submitted (OCT-2017) 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:PHU37747.1}.
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DR   EMBL; PDYG01000030; PHU37747.1; -; Genomic_DNA.
DR   RefSeq; WP_031543328.1; NZ_PDYG01000030.1.
DR   AlphaFoldDB; A0A2G3E397; -.
DR   Proteomes; UP000224563; 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: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 cycle {ECO:0000313|EMBL:PHU37747.1};
KW   Cell division {ECO:0000313|EMBL:PHU37747.1};
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:UP000224563};
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        7..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        49..67
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        79..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        147..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        186..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        263..289
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        301..326
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        338..359
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   369 AA;  40746 MW;  31083175F259A60C CRC64;
     MESKRRFYFD YSLLFILIFL IFFGLVMLYS SSSYLSANKF GDSGHYLKLQ IRNLLFGLVA
     MAFLTFVDYR IWKRWGTALY VLAMLLCLAV YIPGLGRASH GSARWLYLGP ISFQPSEVAK
     VASIFFLAMF IEHAPHAMYS VRNIFKVIIV MFPLVGVVAY MNLSTAIILF GICACMIFVA
     SPKYKPFGVL VISAIMVGAI FVSIAGYRMA RIQTWLHPEN ASGDDVYQTL QGLYAIGSGG
     LFGKGLGQSM QKLGNVPESQ NDFIFTIICE ELGLFGAICT ILLYALILWR MMVIANNAAD
     LYGSLLVVGI MAHLAIQVIL NIAVVTNSIP NTGITLPFIS YGGTSVSILM AEMGVVLGVS
     RQIRLDNIR
//
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