FTSW_SYNY3
ID FTSW_SYNY3 Reviewed; 393 AA.
AC P74180;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 25-MAY-2022, entry version 119.
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=slr1267;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
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}.
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DR EMBL; BA000022; BAA18269.1; -; Genomic_DNA.
DR PIR; S75810; S75810.
DR AlphaFoldDB; P74180; -.
DR SMR; P74180; -.
DR IntAct; P74180; 2.
DR STRING; 1148.1653355; -.
DR PaxDb; P74180; -.
DR PRIDE; P74180; -.
DR EnsemblBacteria; BAA18269; BAA18269; BAA18269.
DR KEGG; syn:slr1267; -.
DR eggNOG; COG0772; Bacteria.
DR InParanoid; P74180; -.
DR OMA; KLWWSNL; -.
DR PhylomeDB; P74180; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0015648; F:lipid-linked peptidoglycan transporter activity; IBA:GO_Central.
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; IBA:GO_Central.
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; IBA:GO_Central.
DR InterPro; IPR018365; Cell_cycle_FtsW-rel_CS.
DR InterPro; IPR001182; FtsW/RodA.
DR PANTHER; PTHR30474; PTHR30474; 1.
DR Pfam; PF01098; FTSW_RODA_SPOVE; 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..393
FT /note="Probable peptidoglycan glycosyltransferase FtsW"
FT /id="PRO_0000062712"
FT TOPO_DOM 1..30
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 52..60
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 82..84
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 106..119
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 141..157
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..181
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 203..242
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 263..285
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 307..318
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 340..350
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 372..393
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 393 AA; 43038 MW; C02CFFCB98D2F5A4 CRC64;
MITAANLLRI IFPFYDPEVL RWSGEARLMR TLFFAWMAMG VVVLFSASYA ESLDTSGTGL
SIILKQIAYL WLGLNIFNFL VRLPLQVCLK LVPWFLIVVL LLIFLTKSGL GVEVNGARRW
ISLGPILIQP SEFMKPCLVL QAANLFGNWH RFPWRSRLIW LGIFALTLGS ILLQPNLSTT
ALCGMGLWLI ALASGLPWIY LISTALLGIT TAVTSISIRD YQRARVTSFL DPFADPRGDG
YQLVQSLYAI ASGGVLGRGF GMSQQKLFYL PIQTTDFIFA VFAEEFGLVG CITFLAFLGL
FTTMGLRVAM RCRHRVKRLI GLGVVIFLVG QSLLNIGVAS GALPTTGLPL PFFSYGGSSC
LSSLVLAGLL VRVARESNEA EVIPLGTKTA PAV
