ID   FTSW_CYAPA              Reviewed;         397 AA.
AC   P48280;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=Putative 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=Peptidoglycan polymerase {ECO:0000250|UniProtKB:P39604};
DE            Short=PG polymerase {ECO:0000250|UniProtKB:P39604};
GN   Name=ftsW;
OS   Cyanophora paradoxa.
OG   Plastid; Cyanelle.
OC   Eukaryota; Glaucocystophyceae; Cyanophoraceae; Cyanophora.
OX   NCBI_TaxID=2762;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTEX LB 555 / Pringsheim;
RA   Stirewalt V.L., Michalowski C.B., Loeffelhardt W., Bohnert H.J.,
RA   Bryant D.A.;
RT   "Nucleotide sequence of the cyanelle DNA from Cyanophora paradoxa.";
RL   Plant Mol. Biol. Rep. 13:327-332(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTEX LB 555 / Pringsheim;
RA   Loeffelhardt W., Stirewalt V.L., Michalowski C.B., Annarella M.,
RA   Farley J.Y., Schluchter W.M., Chung S., Newmann-Spallart C., Steiner J.M.,
RA   Jakowitsch J., Bohnert H.J., Bryant D.A.;
RT   "The complete sequence of the cyanelle genome of Cyanophora paradoxa: the
RT   genetic complexity of a primitive plastid.";
RL   (In) Schenk H.E.A., Herrmann R., Jeon K.W., Mueller N.E., Schwemmler W.
RL   (eds.);
RL   Eukaryotism and symbiosis, pp.40-48, Springer-Verlag, Heidelberg (1997).
CC   -!- FUNCTION: Could play a role in cyanelle division/peptidoglycan
CC       biosynthesis.
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   -!- SUBCELLULAR LOCATION: Plastid, cyanelle membrane {ECO:0000305}; Multi-
CC       pass membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the SEDS family. {ECO:0000305}.
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DR   EMBL; U30821; AAA81300.1; -; Genomic_DNA.
DR   PIR; T06957; T06957.
DR   RefSeq; NP_043269.1; NC_001675.1.
DR   AlphaFoldDB; P48280; -.
DR   SMR; P48280; -.
DR   GeneID; 801587; -.
DR   GO; GO:0033113; C:cyanelle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051301; P:cell division; IEA:InterPro.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
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 shape; Cyanelle; Glycosyltransferase; Membrane;
KW   Peptidoglycan synthesis; Plastid; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..397
FT                   /note="Putative peptidoglycan glycosyltransferase FtsW"
FT                   /id="PRO_0000062713"
FT   TRANSMEM        46..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        82..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        109..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        174..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        198..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        302..322
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        339..359
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        367..387
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   397 AA;  45334 MW;  2567C733BFB98086 CRC64;
     MQLLYTILKE IADAILFFFI QVFKIFRYFF YPEFKNCSKL ATLLRWLTHF WLFFGLMVLI
     SASGFTSYEE HRDVLYYFKR QFVFCLIGIV ISNILMHFPL TLLLKYSNIP FFFIFGLTIL
     TLMPNIGISI NGARRWIAVY GFLVQPSELI KPFWVLQISK IFGQWEFLTT RTKIFWLIIF
     LIQIVAVLIQ PNLSTASLLG ITLWLMGLCA NFPWKYLLGT VFVGLSMAIT SISLKPYQLS
     RITSFLDPWK DPRGKGYQLV QSLITIGSGG IFGTGYGISL QKTGYLPIHY TDFIFAVYIE
     EFGFIGAVSL LLLIIFYFLL VITVILKTNH PVLRLVGCGA IILLMIQTLL NMAVATGIFP
     TTGLPLPFFS YGGNALLANL INCSFLIRLA LETKDRN