FTSW_MESVI
ID FTSW_MESVI Reviewed; 415 AA.
AC Q9MUM4;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Putative peptidoglycan glycosyltransferase FtsW {ECO:0000250|UniProtKB:O07639};
DE Short=PGT {ECO:0000250|UniProtKB:O07639};
DE EC=2.4.1.129 {ECO:0000250|UniProtKB:O07639};
DE AltName: Full=Peptidoglycan polymerase {ECO:0000250|UniProtKB:O07639};
DE Short=PG polymerase {ECO:0000250|UniProtKB:O07639};
GN Name=ftsW;
OS Mesostigma viride (Green alga).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Mesostigmatophyceae;
OC Mesostigmatales; Mesostigmataceae; Mesostigma.
OX NCBI_TaxID=41882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-296 / KY-14 / CCMP 2046;
RX PubMed=10688199; DOI=10.1038/35001059;
RA Lemieux C., Otis C., Turmel M.;
RT "Ancestral chloroplast genome in Mesostigma viride reveals an early branch
RT of green plant evolution.";
RL Nature 403:649-652(2000).
CC -!- FUNCTION: Could play a role in chloroplast 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, chloroplast membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the SEDS family. {ECO:0000305}.
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DR EMBL; AF166114; AAF43874.1; -; Genomic_DNA.
DR RefSeq; NP_038436.1; NC_002186.1.
DR AlphaFoldDB; Q9MUM4; -.
DR SMR; Q9MUM4; -.
DR GeneID; 800983; -.
DR GO; GO:0031969; C:chloroplast 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; Chloroplast; Glycosyltransferase; Membrane;
KW Peptidoglycan synthesis; Plastid; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..415
FT /note="Putative peptidoglycan glycosyltransferase FtsW"
FT /id="PRO_0000062714"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..358
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..387
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 415 AA; 46814 MW; E35116E9692EC782 CRC64;
MIRRFVSICI QLIEDLLIGG WNSIWYYLFP IMHPRCANWW SVARWLQWLT FLWLSIGLIV
LCSASYPSAQ FEFNDGLYYV KRQLLWTILG ILEFNLLTRL LIKDILKISS LGIIFSFLCL
LLTFPMGISV NGASRWIAIG PILLQPSEII KPFLILQSSY IFSQWDNISY SKKIFWVILF
ISIIGSILIQ PNLSTASLCG AIIWLVALTA GIHWFYLNSI LSIGAVTALI SLGSQEYQRQ
RIISFLNPWA NPTSIGYQLV QSLLAVGSGR LTGSGISCSY QKLFYLPIQY TDFIFSVFSE
EFGLLGAFLF ISLLIIYFSL GMIVVLSNKS KVNRLLALGC IMVLVGQSLI NIGVSVGILP
TTGLPLPFFS YGGNSILATF FVSAILIRVA IETEIDNRIN IFSLLNKQSI FYWFK