FTSW_THICA
ID FTSW_THICA Reviewed; 388 AA.
AC F6D9Q8;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 1.
DT 25-MAY-2022, entry version 45.
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=Thicy_1343;
OS Thiomicrospira cyclica (strain DSM 14477 / JCM 11371 / ALM1)
OS (Thioalkalimicrobium cyclicum).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Thiomicrospira.
OX NCBI_TaxID=717773;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14477 / JCM 11371 / ALM1;
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Davenport K., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Kappler U., Woyke T.;
RT "Complete sequence of Thioalkalimicrobium cyclicum ALM1.";
RL Submitted (MAY-2011) 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}.
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DR EMBL; CP002776; AEG32107.1; -; Genomic_DNA.
DR RefSeq; WP_013835883.1; NC_015581.1.
DR AlphaFoldDB; F6D9Q8; -.
DR SMR; F6D9Q8; -.
DR STRING; 717773.Thicy_1343; -.
DR EnsemblBacteria; AEG32107; AEG32107; Thicy_1343.
DR KEGG; tcy:Thicy_1343; -.
DR eggNOG; COG0772; Bacteria.
DR HOGENOM; CLU_029243_0_1_6; -.
DR OMA; KLWWSNL; -.
DR OrthoDB; 1133883at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000009232; Chromosome.
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..388
FT /note="Probable peptidoglycan glycosyltransferase FtsW"
FT /id="PRO_0000415214"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TRANSMEM 310..330
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
SQ SEQUENCE 388 AA; 42279 MW; 038E6BE1EFF1FC8F CRC64;
MANTWRLDIR GLDGSLVLIV LALITIGLVM VLSSSVAVSE VRFGHQWHYF QRQVFALGVG
GLFAALVLMV PSQSWLQHRG KWFLLGLVLL ALVLIFGREI GGAKRWLPLV VMNFQPAEWM
KIATILFLAG YLQRHQDAVK QDSTAVIRLF LPFGIMAGLL LLQPDYGTTV LIAGVLVGML
FIAGAPFRYF VITVLPIGAI LAVLLINSPY RMARVMNFMD PWQDPYGVGY QLSQALMAIG
SGGITGSGLG ASVQKLLYLP DAHTDFMFAV FAEETGWLGV VILLSLYGLL LWRMFAVAQA
AWLPQAPFKA LVVYGVAIMF AGQLLINVGV NLGVFPTKGL TLPFVSYGGS SLMMALLAIG
LVLRIDYETR LIKGHSTEEL SANPSFGS
