FTSW_CAUVN
ID FTSW_CAUVN Reviewed; 390 AA.
AC B8H092;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 64.
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=CCNA_02635;
OS Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=565050;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1000 / CB15N;
RX PubMed=20472802; DOI=10.1128/jb.00255-10;
RA Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA Walunas T.L., Crosson S.;
RT "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL J. Bacteriol. 192:3678-3688(2010).
RN [2]
RP INTERACTION WITH FTSI; FTSN AND SIDA, AND MUTAGENESIS OF PHE-145 AND
RP THR-180.
RC STRAIN=NA1000 / CB15N;
RX PubMed=21685367; DOI=10.1101/gad.2038911;
RA Modell J.W., Hopkins A.C., Laub M.T.;
RT "A DNA damage checkpoint in Caulobacter crescentus inhibits cell division
RT through a direct interaction with FtsW.";
RL Genes Dev. 25:1328-1343(2011).
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 -!- SUBUNIT: Interacts with FtsI, FtsN and the cell division inhibitor
CC SidA. {ECO:0000269|PubMed:21685367}.
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; CP001340; ACL96100.1; -; Genomic_DNA.
DR RefSeq; WP_010920409.1; NC_011916.1.
DR RefSeq; YP_002518008.1; NC_011916.1.
DR AlphaFoldDB; B8H092; -.
DR SMR; B8H092; -.
DR DIP; DIP-61066N; -.
DR IntAct; B8H092; 2.
DR PRIDE; B8H092; -.
DR EnsemblBacteria; ACL96100; ACL96100; CCNA_02635.
DR GeneID; 7332737; -.
DR KEGG; ccs:CCNA_02635; -.
DR PATRIC; fig|565050.3.peg.2583; -.
DR HOGENOM; CLU_029243_1_1_5; -.
DR OMA; KLWWSNL; -.
DR OrthoDB; 1133883at2; -.
DR PhylomeDB; B8H092; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001364; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-KW.
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; IEA:UniProtKB-KW.
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.
PE 1: Evidence at protein level;
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..390
FT /note="Probable peptidoglycan glycosyltransferase FtsW"
FT /id="PRO_0000420268"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..299
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..335
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 348..368
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MUTAGEN 145
FT /note="F->L: Decreases interaction with SidA."
FT /evidence="ECO:0000269|PubMed:21685367"
FT MUTAGEN 180
FT /note="T->A: Decreases interaction with SidA."
FT /evidence="ECO:0000269|PubMed:21685367"
SQ SEQUENCE 390 AA; 42014 MW; 282DFE558231AB36 CRC64;
MASNATHAFA RTDRTALGLW WWTTDRWLLG ATALLVTLGM LLSFASSPAA AQRIGIDDQF
HFALRMCFFA TASSVLMLIT SMLSPRDIRR AAFFIYLGAI AVMIALPFIG HNAKGATRWL
QFAGFTLQPS EFMKPALIVL VSWMFAEGQK GEGVPGVSIA FLLYFIAVAL LLIQPDVGQT
VLITIAFGAA FWMAGVPISW IMGLGGVALA GLGSTYFLFD HVHARVQKFL SPDQADTHQI
TRAAEAIRAG GLFGRGPGEG VMKRHVPDLH TDFIYSVAAE EYGLIFSWSL IGLFAFVVVR
GLYKAMKLND PFEQVAAAGL FVLVGQQALI NIAVNLNMIP TKGMTLPFIS YGGSSMLAMG
LTLGMALALL RKRPGAYGAS GEFGFGRADA
