FTSW_LACLC
ID FTSW_LACLC Reviewed; 198 AA.
AC P27174;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 3.
DT 25-MAY-2022, entry version 79.
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};
DE Flags: Fragment;
GN Name=ftsW;
OS Lactococcus lactis subsp. cremoris (Streptococcus cremoris).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=1359;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MG1614;
RX PubMed=1398083; DOI=10.1016/0378-1119(92)90081-y;
RA Koivula T., Hemilae H.;
RT "Sequence encoding ribosomal protein L33 of Lactococcus lactis.";
RL Gene 119:145-146(1992).
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 membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000255}. Note=Localizes to the division septum.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SEDS family. FtsW subfamily. {ECO:0000305}.
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DR EMBL; X62621; CAA44490.1; -; Genomic_DNA.
DR PIR; PC1134; PC1134.
DR AlphaFoldDB; P27174; -.
DR UniPathway; UPA00219; -.
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; IPR001182; FtsW/RodA.
DR PANTHER; PTHR30474; PTHR30474; 1.
DR Pfam; PF01098; FTSW_RODA_SPOVE; 1.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Cell membrane; Cell shape;
KW Cell wall biogenesis/degradation; Glycosyltransferase; Membrane;
KW Peptidoglycan synthesis; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..>198
FT /note="Probable peptidoglycan glycosyltransferase FtsW"
FT /id="PRO_0000062708"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT NON_TER 198
SQ SEQUENCE 198 AA; 22102 MW; 8435716E63796694 CRC64;
MNLNKNNFLN YSILIPYLIL AGIGIVMIFS TTVPDQLQKG LNPYKLVINQ TAFVLLSIIM
IAVIYRLKLR ALKNRKMIGI IMVILILSLI FCRIMPSSFA LTAPVNGARG WIHIPGIGTV
QPAEFAKVFI IWYLASVFST KQEEIEKNDI NEIFKGKTLT QKLFGGWRLP VVAILLVDLI
MPDLGNTMII GAVALIMI
