(data stored in ACNUC7421 zone)

SWISSPROT: FTSW_SHESH

ID   FTSW_SHESH              Reviewed;         410 AA.
AC   A8FQ99;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 56.
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=Ssed_0409;
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Peptidoglycan polymerase that is essential for cell
CC       division. {ECO:0000255|HAMAP-Rule:MF_00913}.
CC   -!- CATALYTIC ACTIVITY: (GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-
CC       Lys-D-Ala-D-Ala))(n)-diphosphoundecaprenol + GlcNAc-(1->4)-
CC       Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-
CC       diphosphoundecaprenol = (GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-
CC       Glu-L-Lys-D-Ala-D-Ala))(n+1)-diphosphoundecaprenol + undecaprenyl
CC       diphosphate. {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; CP000821; ABV35022.1; -; Genomic_DNA.
DR   RefSeq; WP_012140759.1; NC_009831.1.
DR   STRING; 425104.Ssed_0409; -.
DR   EnsemblBacteria; ABV35022; ABV35022; Ssed_0409.
DR   KEGG; sse:Ssed_0409; -.
DR   eggNOG; ENOG4105CNI; Bacteria.
DR   eggNOG; COG0772; LUCA.
DR   HOGENOM; HOG000282689; -.
DR   KO; K03588; -.
DR   OMA; KGYQLSH; -.
DR   OrthoDB; POG091H06AB; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000002015; 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   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; A8FQ99.
DR   SWISS-2DPAGE; A8FQ99.
KW   Cell cycle; Cell division; Cell inner membrane; Cell membrane;
KW   Cell shape; Cell wall biogenesis/degradation; Complete proteome;
KW   Glycosyltransferase; Membrane; Peptidoglycan synthesis; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    410       Probable peptidoglycan
FT                                glycosyltransferase FtsW.
FT                                /FTId=PRO_0000415212.
FT   TOPO_DOM      1     37       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM     38     58       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00913}.
FT   TOPO_DOM     59     69       Periplasmic. {ECO:0000255}.
FT   TRANSMEM     70     90       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00913}.
FT   TOPO_DOM     91     99       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    100    120       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00913}.
FT   TOPO_DOM    121    131       Periplasmic. {ECO:0000255}.
FT   TRANSMEM    132    154       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00913}.
FT   TOPO_DOM    155    163       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    164    184       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00913}.
FT   TOPO_DOM    185    186       Periplasmic. {ECO:0000255}.
FT   TRANSMEM    187    207       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00913}.
FT   TOPO_DOM    208    208       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    209    229       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00913}.
FT   TOPO_DOM    230    291       Periplasmic. {ECO:0000255}.
FT   TRANSMEM    292    312       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00913}.
FT   TOPO_DOM    313    336       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    337    357       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00913}.
FT   TOPO_DOM    358    364       Periplasmic. {ECO:0000255}.
FT   TRANSMEM    365    385       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00913}.
FT   TOPO_DOM    386    410       Cytoplasmic. {ECO:0000255}.
SQ   SEQUENCE   410 AA;  45693 MW;  A06E0EC90C4CC4F4 CRC64;
     MRSEERQLNL FGTSVNWSWP NLFKEREAPG MQLYDRALLF AVLSLICFGF VMVMSASMPE
     AQSLTGNPYH FAIRHFAYLV GCAVIAAVVL RIEMSRWQQF SPLLLLIVGI MLVAVLLVGT
     SVNGATRWLS VGPIRIQVAE LAKFAFTIYM AGYLVRRHQE IRENAKGFYK PIAVFAVYAF
     LILMQPDLGT VVVLFVGTVG LLFLAGARLL DFFALILTGV MAFVALVLLE PYRMRRVTSF
     MDPWQDPFGS GYQLTQSLMA YGRGDWFGQG LGNSIQKLEY LPEAHTDFIF AVIGEELGFI
     GIVVVLSVLL FVALRAIKLG NLCIEIDKPF EGYLAYAIGI WFCFQTVVNV GASIGMLPTK
     GLTLPFISYG GSSLWVMTAA AMILIRIDHE RRLSSIQAVQ GKKVNDNREY
//

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