FTSW_THISH
ID FTSW_THISH Reviewed; 400 AA.
AC B8GMM8;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 60.
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=Tgr7_0768;
OS Thioalkalivibrio sulfidiphilus (strain HL-EbGR7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Thioalkalivibrio.
OX NCBI_TaxID=396588;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL-EbGR7;
RX PubMed=21475584; DOI=10.4056/sigs.1483693;
RA Muyzer G., Sorokin D.Y., Mavromatis K., Lapidus A., Clum A., Ivanova N.,
RA Pati A., d'Haeseleer P., Woyke T., Kyrpides N.C.;
RT "Complete genome sequence of 'Thioalkalivibrio sulfidophilus' HL-EbGr7.";
RL Stand. Genomic Sci. 4:23-35(2011).
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; CP001339; ACL71860.1; -; Genomic_DNA.
DR RefSeq; WP_012637348.1; NC_011901.1.
DR AlphaFoldDB; B8GMM8; -.
DR SMR; B8GMM8; -.
DR STRING; 396588.Tgr7_0768; -.
DR EnsemblBacteria; ACL71860; ACL71860; Tgr7_0768.
DR KEGG; tgr:Tgr7_0768; -.
DR eggNOG; COG0772; Bacteria.
DR HOGENOM; CLU_029243_1_1_6; -.
DR OMA; KLWWSNL; -.
DR OrthoDB; 1133883at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000002383; 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; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..400
FT /note="Probable peptidoglycan glycosyltransferase FtsW"
FT /id="PRO_0000415215"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TRANSMEM 65..84
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TRANSMEM 356..376
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
SQ SEQUENCE 400 AA; 42652 MW; 6561E32EDC321C6B CRC64;
MSAVDIQATR DAGQQLQVRL AQRLDLGLTL SVLALLGLGL VMVASASIGI ADRNLGDPLY
FLKRQAAYVV LGLAAASLAY RIRLAYWEAS AGLLLGFAYF LLILVLVPGV GVTVNGSTRW
LSLGLFNLQV SEVAKLLFTL YLAGYLTRHG RAVREQFAGF LRPMLLLSGA ALLLLMEPDF
GAAVVLMAIG LALLFLAGAK LWQFALLVGT VAAALAMLAI TTPYRMARLT AFLDPWNDPF
NSGFQLTQSL IAIGSGSWFG VGLGASVQKL FYLPEAHNDF LFAVLAEELG LVGITVVVLL
YGWFLWRSFG IGRAAEQAGQ LFGAYLAYGV GVWVSLQAFI NMGVNMGLLP TKGLTLPLMS
YGGSSMLMTC AAVGLLLRVH RETVESGPLR VGRVTGGRGA
