FTSW_BORBU
ID FTSW_BORBU Reviewed; 364 AA.
AC Q44775; Q44874; Q44922;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Probable peptidoglycan glycosyltransferase FtsW {ECO:0000250|UniProtKB:P39604};
DE Short=PGT {ECO:0000250|UniProtKB:P39604};
DE EC=2.4.1.129 {ECO:0000250|UniProtKB:P39604};
DE AltName: Full=Cell division protein FtsW {ECO:0000250|UniProtKB:O07639};
DE AltName: Full=Cell wall polymerase {ECO:0000250|UniProtKB:P39604};
DE AltName: Full=Peptidoglycan polymerase {ECO:0000250|UniProtKB:P39604};
DE Short=PG polymerase {ECO:0000250|UniProtKB:P39604};
GN Name=ftsW; OrderedLocusNames=BB_0302;
OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS (Borrelia burgdorferi).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=224326;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RA Dunn J.J., Butler-Loffredo L., Kieleczawa J., Medalle J., Luft B.J.;
RL Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=212;
RA Ge Y., Old I.G., Saint Girons I., Charon N.W.;
RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX PubMed=9403685; DOI=10.1038/37551;
RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA Smith H.O., Venter J.C.;
RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL Nature 390:580-586(1997).
CC -!- FUNCTION: Peptidoglycan polymerase that is essential for cell division.
CC {ECO:0000250|UniProtKB:P39604}.
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:0000250|UniProtKB:P39604};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000250|UniProtKB:P39604}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000255}. Note=Localizes to the division septum.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SEDS family. FtsW subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC66646.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U43739; AAA85625.1; -; Genomic_DNA.
DR EMBL; X96685; CAA65461.1; -; Genomic_DNA.
DR EMBL; X96433; CAA65294.1; -; Genomic_DNA.
DR EMBL; AE000783; AAC66646.2; ALT_INIT; Genomic_DNA.
DR PIR; F70137; F70137.
DR RefSeq; NP_212436.2; NC_001318.1.
DR RefSeq; WP_002657744.1; NC_001318.1.
DR AlphaFoldDB; Q44775; -.
DR SMR; Q44775; -.
DR STRING; 224326.BB_0302; -.
DR PRIDE; Q44775; -.
DR EnsemblBacteria; AAC66646; AAC66646; BB_0302.
DR KEGG; bbu:BB_0302; -.
DR PATRIC; fig|224326.49.peg.701; -.
DR HOGENOM; CLU_029243_1_2_12; -.
DR OMA; KLWWSNL; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001807; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR InterPro; IPR018365; Cell_cycle_FtsW-rel_CS.
DR InterPro; IPR013437; FtsW.
DR InterPro; IPR001182; FtsW/RodA.
DR PANTHER; PTHR30474; PTHR30474; 1.
DR Pfam; PF01098; FTSW_RODA_SPOVE; 1.
DR TIGRFAMs; TIGR02614; ftsW; 1.
DR PROSITE; PS00428; FTSW_RODA_SPOVE; 1.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Cell inner membrane; Cell membrane; Cell shape;
KW Cell wall biogenesis/degradation; Glycosyltransferase; Membrane;
KW Peptidoglycan synthesis; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..364
FT /note="Probable peptidoglycan glycosyltransferase FtsW"
FT /id="PRO_0000062696"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..43
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 65..74
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..100
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..136
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 158..160
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 203..271
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 272..292
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 293..301
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 323..333
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 334..354
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 355..364
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CONFLICT 98
FT /note="A -> P (in Ref. 2; CAA65461)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 364 AA; 40950 MW; CB80973C50BF040A CRC64;
MVVEINSLRT CYLLVLLLLV AYGLVVFYTS SFFLSLELTG NPNFLFFTRL NYLFLSFMVF
LVFERISLNF LKKSIFPVLI ITLFLIMATF LSPSISGAKR WIFFQGVSIQ PSEIFKISFT
IYLSAYLSKF DPRKNNGISY WIKPMLIFAI FWVLIILQND YSTAIYFAIL FFIVLFVSNM
AFSYVFAIVV TFLPVSAIFL MLEPYRVSRI FAFLNPYDDP SGKGYQIIAS LNALKSGGIL
GKGLGMGEVK LGKLPEANSD FIFSVLGEEL GFLGVLFAIS LFFLFFYFGY FIAIHSNSRF
KFFIAFISSL AIFLQSMMNI LIAIGLLPPT GINLPFFSSG GSSIIVTMAL SGLISNVSKN
LSNN
