FTSW_THIK1
ID FTSW_THIK1 Reviewed; 411 AA.
AC D5X4H4;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 1.
DT 03-AUG-2022, entry version 50.
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=Tint_0364;
OS Thiomonas intermedia (strain K12) (Thiobacillus intermedius).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Thiomonas.
OX NCBI_TaxID=75379;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ovchinnikova G., Kerfeld C.A., Cannon G.C.,
RA Heinhorst S., Woyke T.;
RT "Complete sequence of Thiomonas intermedia K12.";
RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002021; ADG29775.1; -; Genomic_DNA.
DR RefSeq; WP_013122142.1; NC_014153.1.
DR AlphaFoldDB; D5X4H4; -.
DR SMR; D5X4H4; -.
DR STRING; 75379.Tint_0364; -.
DR EnsemblBacteria; ADG29775; ADG29775; Tint_0364.
DR KEGG; tin:Tint_0364; -.
DR eggNOG; COG0772; Bacteria.
DR HOGENOM; CLU_029243_1_1_4; -.
DR OMA; KLWWSNL; -.
DR BioCyc; TINT75379:TINT_RS01850-MON; -.
DR UniPathway; UPA00219; -.
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; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..411
FT /note="Probable peptidoglycan glycosyltransferase FtsW"
FT /id="PRO_0000415218"
FT TOPO_DOM 1..40
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TOPO_DOM 62..81
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TOPO_DOM 103..109
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TOPO_DOM 131..136
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TOPO_DOM 158..172
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TOPO_DOM 194..196
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TOPO_DOM 218..219
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TOPO_DOM 241..298
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 299..319
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TOPO_DOM 320..347
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 348..368
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TOPO_DOM 369..374
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..395
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TOPO_DOM 396..411
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 411 AA; 45509 MW; 7863053900B6C222 CRC64;
MLERMLPFLG RKRDKAAADL PVRVGHSAPR NSRMLEYDQN LVWVTLLLLA YGLVMVYSAT
ISFHDSPRYA QWSPYHYFIR DLFSIAAALL ASWIVVQIPM AELQKWSMRF FFLSLIGLVL
VLLPHIGKDV NGSKRWVVFP GGLNFQPSEL VKLTALIYAA DFMVRKQEVK QSLLKTFLPM
MAVMMIVGVL LLAEPDMGAF LVIASITLAI LFLGGANGKL FSVFSVAVIG AFVLMIVLSP
WRRDRIFAYL NPWSESNALG SAYQLSHALI AMGRGEWFGV GLGGSIEKLH YLPEAHTDFL
LAIIGEELGL VGVGVVIFAF YWIVRRAFDI GRQALVLDRM YSALVAQGIG VWIGGQAFIN
IGVNLGLLPT KGLTLPLMSY GGSALLLNCM AIAVLLRVDF ENRILMRGGH V
