FTSW_PSET1
ID FTSW_PSET1 Reviewed; 398 AA.
AC Q3IG03;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Probable peptidoglycan glycosyltransferase FtsW {ECO:0000255|HAMAP-Rule:MF_00913};
DE Short=PGT {ECO:0000255|HAMAP-Rule:MF_00913};
DE EC=2.4.1.129 {ECO:0000255|HAMAP-Rule:MF_00913};
DE AltName: Full=Cell division protein FtsW {ECO:0000255|HAMAP-Rule:MF_00913};
DE AltName: Full=Cell wall polymerase {ECO:0000255|HAMAP-Rule:MF_00913};
DE AltName: Full=Peptidoglycan polymerase {ECO:0000255|HAMAP-Rule:MF_00913};
DE Short=PG polymerase {ECO:0000255|HAMAP-Rule:MF_00913};
GN Name=ftsW {ECO:0000255|HAMAP-Rule:MF_00913}; OrderedLocusNames=PSHAa2505;
OS Pseudoalteromonas translucida (strain TAC 125).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=326442;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TAC 125;
RX PubMed=16169927; DOI=10.1101/gr.4126905;
RA Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G., Ho C.,
RA Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C., Rouy Z.,
RA Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT "Coping with cold: the genome of the versatile marine Antarctica bacterium
RT Pseudoalteromonas haloplanktis TAC125.";
RL Genome Res. 15:1325-1335(2005).
CC -!- FUNCTION: Peptidoglycan polymerase that is essential for cell division.
CC {ECO:0000255|HAMAP-Rule:MF_00913}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00913};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00913}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00913}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00913}. Note=Localizes to the division septum.
CC {ECO:0000255|HAMAP-Rule:MF_00913}.
CC -!- SIMILARITY: Belongs to the SEDS family. FtsW subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00913}.
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DR EMBL; CR954246; CAI87553.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3IG03; -.
DR SMR; Q3IG03; -.
DR STRING; 326442.PSHAa2505; -.
DR EnsemblBacteria; CAI87553; CAI87553; PSHAa2505.
DR KEGG; pha:PSHAa2505; -.
DR eggNOG; COG0772; Bacteria.
DR HOGENOM; CLU_029243_0_1_6; -.
DR OMA; KLWWSNL; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000006843; Chromosome I.
DR GO; GO:0032153; C:cell division site; IEA:UniProtKB-UniRule.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-UniRule.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR HAMAP; MF_00913; PGT_FtsW_proteobact; 1.
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..398
FT /note="Probable peptidoglycan glycosyltransferase FtsW"
FT /id="PRO_0000415208"
FT TOPO_DOM 1..25
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TOPO_DOM 47..69
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TOPO_DOM 91
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TOPO_DOM 113..120
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TOPO_DOM 142..156
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TOPO_DOM 178..179
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TOPO_DOM 201
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TOPO_DOM 223..289
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..312
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TOPO_DOM 313..324
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TOPO_DOM 346..356
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 357..377
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TOPO_DOM 378..398
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 398 AA; 43625 MW; 29E6758A42C84103 CRC64;
MCYGGTAMMA FADIKEALTP KPSAQLYDVP LLYCMLMLMG VGFVMVTSAS MPTADRLFGN
IYHFTIRHGI FLALSFCLFW ITTSVPMSWW KKANPYLLLV GLGLLLIVLI VGREVNGSTR
WIPIGPFNIQ ASELAKLFFF SYISGYLVRK RSEVQENIKG FIKPILVFAA YAGLILMQPD
LGTVVVMFVT TVGLLFLAGA KLWQFFVLIL TGVALVIGLI VLEPYRMARV IGFLEPWDDP
FGKGYQLVQS LMAYSQGDWF GQGLGNSVQK LQYLPEAHTD FIFAVIAEEL GFVGVSSILI
VLGTLVFRAL LIGQNALKNG KEYEGYLALA IGIWFAFQTM VNVGASAGIL PTKGLTLPFI
SYGGSSLLMM TIAAGILLRV DFETKMATKQ ATSGGAKR
