ID O83402_TREPA Unreviewed; 384 AA.
AC O83402;
DT 01-NOV-1998, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1998, sequence version 1.
DT 27-MAR-2024, entry version 123.
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 OrderedLocusNames=TP_0387 {ECO:0000313|EMBL:AAC65371.1};
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC Treponema.
OX NCBI_TaxID=243276 {ECO:0000313|EMBL:AAC65371.1, ECO:0000313|Proteomes:UP000000811};
RN [1] {ECO:0000313|EMBL:AAC65371.1, ECO:0000313|Proteomes:UP000000811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols {ECO:0000313|EMBL:AAC65371.1,
RC ECO:0000313|Proteomes:UP000000811};
RX PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G., Dodson R.,
RA Gwinn M., Hickey E.K., Clayton R., Ketchum K.A., Sodergren E.,
RA Hardham J.M., McLeod M.P., Salzberg S., Peterson J., Khalak H.,
RA Richardson D., Howell J.K., Chidambaram M., Utterback T., McDonald L.,
RA Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S., Hatch B.,
RA Horst K., Roberts K., Watthey L., Weidman J., Smith H.O., Venter J.C.;
RT "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL Science 281:375-388(1998).
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 -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
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}.
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DR EMBL; AE000520; AAC65371.1; -; Genomic_DNA.
DR PIR; E71331; E71331.
DR RefSeq; WP_010881835.1; NC_021490.2.
DR AlphaFoldDB; O83402; -.
DR IntAct; O83402; 7.
DR STRING; 243276.TP_0387; -.
DR EnsemblBacteria; AAC65371; AAC65371; TP_0387.
DR KEGG; tpa:TP_0387; -.
DR PATRIC; fig|243276.9.peg.387; -.
DR eggNOG; COG0772; Bacteria.
DR HOGENOM; CLU_029243_1_2_12; -.
DR OrthoDB; 9768187at2; -.
DR Proteomes; UP000000811; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; 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; IPR013437; FtsW.
DR InterPro; IPR001182; FtsW/RodA.
DR NCBIfam; TIGR02614; ftsW; 1.
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:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000313|EMBL:AAC65371.1};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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:UP000000811};
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 16..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 58..76
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 83..102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 151..169
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 281..305
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 314..335
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 347..368
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 384 AA; 42715 MW; 01DF27E5E30B4F2E CRC64;
MRPMISIEKN VHQERYSFVF ILLVALMVGV GFVTLYSGSV HYAQRFFRYP GYFLVRQGVS
IGIGLVCLLF FTFVRLASLR KALSPLILVA FALCVCTFFP GIGSTRNGAT RWIKVFDINF
QPSEFVKLVL IVFLANFFDK HREHFDTPIR SIFPPFVVSV IFVSVVFFQN DFSTAMFLLF
ITVVMFFIAG APLWWFLRGI MVLAPIAVLM IVTSTNRLRR VLSFLYPDRD PLGAGYQVNA
ALEALMDGGL WGRGIGNGVR KIASVPEVYS DFIFVVIGEE MGFIGVCLYL MLLFAFTLTG
ISIALRCANR FNTFLAFGAS AAIVLQSILN VAVVVRLVPA TGIPLPFFSS GGSSIVVTLS
LCGLIINVSG DEKIRREREE TVFV
//
