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FTSW_GEOS8
ID   FTSW_GEOS8              Reviewed;         367 AA.
AC   E8WSG3;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 1.
DT   25-MAY-2022, entry version 50.
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}; OrderedLocusNames=GM18_3888;
OS   Geobacter sp. (strain M18).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Geobacter; unclassified Geobacter.
OX   NCBI_TaxID=443143;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M18;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Chertkov O., Munk C., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Holmes D.,
RA   Aklujkar M., Lovley D., Woyke T.;
RT   "Complete sequence of Geobacter sp. M18.";
RL   Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Peptidoglycan polymerase that is essential for cell division.
CC       {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-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; Evidence={ECO:0000255|HAMAP-
CC         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}.
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DR   EMBL; CP002479; ADW15310.1; -; Genomic_DNA.
DR   AlphaFoldDB; E8WSG3; -.
DR   SMR; E8WSG3; -.
DR   STRING; 443143.GM18_3888; -.
DR   EnsemblBacteria; ADW15310; ADW15310; GM18_3888.
DR   KEGG; geb:GM18_3888; -.
DR   eggNOG; COG0772; Bacteria.
DR   HOGENOM; CLU_029243_0_1_7; -.
DR   OMA; KLWWSNL; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001442; 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;
KW   Cell cycle; Cell division; Cell inner membrane; Cell membrane; Cell shape;
KW   Cell wall biogenesis/degradation; Glycosyltransferase; Membrane;
KW   Peptidoglycan synthesis; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..367
FT                   /note="Probable peptidoglycan glycosyltransferase FtsW"
FT                   /id="PRO_0000415184"
FT   TOPO_DOM        1..8
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT   TOPO_DOM        30..49
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        50..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT   TOPO_DOM        71..72
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        73..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT   TOPO_DOM        94..138
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        139..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT   TOPO_DOM        160..161
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        162..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT   TOPO_DOM        183
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        184..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT   TOPO_DOM        205..225
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        226..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT   TOPO_DOM        247..266
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        267..287
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT   TOPO_DOM        288..304
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        305..325
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT   TOPO_DOM        326..335
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        336..356
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT   TOPO_DOM        357..367
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   367 AA;  40172 MW;  B81B7973179FBADD CRC64;
     MRRVEGYDMI VLMMAVILTC FGVVMVYSAS SVMAAKKFHD GFFFLKRQSL YALIGFIGMG
     VAMHVDYHVW KKWAVPLFLG TFFLLLLVFV PGIGGTAKGA SRWIRLPGFN FQPSELAKVA
     LIMYMAYSLE KRQDKLKQFM SGFFPYMLIL GVFIAVLLAQ HDMGAALTML AVAIVMLFAA
     GTKVQYILGM GLVALPGICY LVFTKAYRMR RITAFLDPWQ DPTDAGFQII QSWLALGTGG
     FFGQGLGEGK QKLFYLPEAH TDFILSVLGE EMGFIGVVVI ASMFLLLVQR SIRVAIAAED
     SFGRFLAFGI AILLGLEAFV NMAVVTGLLP TKGIALPFLS YGGSSLIISL CSVGVLLNVS
     TRMRGAA
 
 
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