(data stored in ACNUC7421 zone)

SWISSPROT: FTSW_ECO57

ID   FTSW_ECO57              Reviewed;         414 AA.
AC   P0ABG6; P16457;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   08-MAY-2019, entry version 90.
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};
GN   OrderedLocusNames=Z0099, ECs0093;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Peptidoglycan polymerase that is essential for cell
CC       division. {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-
CC         D-Ala)](n)-diphospho-di-trans,octa-cis-undecaprenol + beta-D-
CC         GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-
CC         diphospho-di-trans,octa-cis-undecaprenol = [GlcNAc-(1->4)-
CC         Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-diphospho-
CC         di-trans-octa-cis-undecaprenol + di-trans,octa-cis-undecaprenyl
CC         diphosphate + H(+); Xref=Rhea:RHEA:23708, Rhea:RHEA-COMP:9602,
CC         Rhea:RHEA-COMP:9603, ChEBI:CHEBI:15378, ChEBI:CHEBI:58405,
CC         ChEBI:CHEBI:60033, ChEBI:CHEBI:78435; EC=2.4.1.129;
CC         Evidence={ECO:0000255|HAMAP-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}.
DR   EMBL; AE005174; AAG54393.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33516.1; -; Genomic_DNA.
DR   PIR; E85491; E85491.
DR   PIR; E90640; E90640.
DR   RefSeq; NP_308120.1; NC_002695.1.
DR   RefSeq; WP_001295532.1; NZ_SDVX01000001.1.
DR   STRING; 155864.EDL933_0092; -.
DR   PRIDE; P0ABG6; -.
DR   EnsemblBacteria; AAG54393; AAG54393; Z0099.
DR   EnsemblBacteria; BAB33516; BAB33516; BAB33516.
DR   GeneID; 913549; -.
DR   KEGG; ece:Z0099; -.
DR   KEGG; ecs:ECs0093; -.
DR   PATRIC; fig|386585.9.peg.193; -.
DR   eggNOG; ENOG4105CNI; Bacteria.
DR   eggNOG; COG0772; LUCA.
DR   HOGENOM; HOG000282689; -.
DR   KO; K03588; -.
DR   BioCyc; ECOO157:FTSW-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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;
DR   PRODOM; P0ABG6.
DR   SWISS-2DPAGE; P0ABG6.
KW   Cell cycle; Cell division; Cell inner membrane; Cell membrane;
KW   Cell shape; Cell wall biogenesis/degradation; Complete proteome;
KW   Glycosyltransferase; Membrane; Peptidoglycan synthesis;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN         1    414       Probable peptidoglycan
FT                                glycosyltransferase FtsW.
FT                                /FTId=PRO_0000062701.
FT   TOPO_DOM      1     12       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM     13     33       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00913}.
FT   TOPO_DOM     34     47       Periplasmic. {ECO:0000255}.
FT   TRANSMEM     48     68       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00913}.
FT   TOPO_DOM     69     86       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM     87    107       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00913}.
FT   TOPO_DOM    108    111       Periplasmic. {ECO:0000255}.
FT   TRANSMEM    112    132       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00913}.
FT   TOPO_DOM    133    174       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    175    194       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00913}.
FT   TOPO_DOM    195    197       Periplasmic. {ECO:0000255}.
FT   TRANSMEM    198    217       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00913}.
FT   TOPO_DOM    218    218       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    219    239       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00913}.
FT   TOPO_DOM    240    301       Periplasmic. {ECO:0000255}.
FT   TRANSMEM    302    322       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00913}.
FT   TOPO_DOM    323    342       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    343    363       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00913}.
FT   TOPO_DOM    364    373       Periplasmic. {ECO:0000255}.
FT   TRANSMEM    374    394       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00913}.
FT   TOPO_DOM    395    414       Cytoplasmic. {ECO:0000255}.
SQ   SEQUENCE   414 AA;  45987 MW;  7935EC952AD9A1F3 CRC64;
     MRLSLPRLKM PRLPGFSILV WISTALKGWV MGSREKDTDS LIMYDRTLLW LTFGLAAIGF
     IMVTSASMPI GQRLTNDPFF FAKRDGVYLI LAFILAIITL RLPMEFWQRY SATMLLGSII
     LLMIVLVVGS SVKGASRWID LGLLRIQPAE LTKLSLFCYI ANYLVRKGDE VRNNLRGFLK
     PMGVILVLAV LLLAQPDLGT VVVLFVTTLA MLFLAGAKLW QFIAIIGMGI SAVVLLILAE
     PYRIRRVTAF WNPWEDPFGS GYQLTQSLMA FGRGELWGQG LGNSVQKLEY LPEAHTDFIF
     AIIGEELGYV GVVLALLMVF FVAFRAMSIG RKALEIDHRF SGFLACSIGI WFSFQALVNV
     GAAAGMLPTK GLTLPLISYG GSSLLIMSTA IMMLLRIDYE TRLEKAQAFV RGSR
//

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