(data stored in SCRATCH zone)

SWISSPROT: Q3Z5S0_SHISS

ID   Q3Z5S0_SHISS            Unreviewed;       414 AA.
AC   Q3Z5S0;
DT   27-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 84.
DE   RecName: Full=Probable peptidoglycan glycosyltransferase FtsW {ECO:0000256|HAMAP-Rule:MF_00913};
DE            Short=PGT {ECO:0000256|HAMAP-Rule:MF_00913};
DE            EC=2.4.1.129 {ECO:0000256|HAMAP-Rule:MF_00913};
DE   AltName: Full=Cell division protein FtsW {ECO:0000256|HAMAP-Rule:MF_00913};
DE   AltName: Full=Cell wall polymerase {ECO:0000256|HAMAP-Rule:MF_00913};
DE   AltName: Full=Peptidoglycan polymerase {ECO:0000256|HAMAP-Rule:MF_00913};
DE            Short=PG polymerase {ECO:0000256|HAMAP-Rule:MF_00913};
GN   Name=ftsW {ECO:0000256|HAMAP-Rule:MF_00913,
GN   ECO:0000313|EMBL:AAZ86892.1};
GN   OrderedLocusNames=SSON_0097 {ECO:0000313|EMBL:AAZ86892.1};
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269 {ECO:0000313|EMBL:AAZ86892.1, ECO:0000313|Proteomes:UP000002529};
RN   [1] {ECO:0000313|EMBL:AAZ86892.1, ECO:0000313|Proteomes:UP000002529}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ss046 {ECO:0000313|EMBL:AAZ86892.1,
RC   ECO:0000313|Proteomes:UP000002529};
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA   Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA   Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA   Qiang B., Hou Y., Yu J., Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic
RT   agents of bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
CC   -!- FUNCTION: Peptidoglycan polymerase that is essential for cell
CC       division. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00913};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00913}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_00913}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_00913}. Note=Localizes to the division septum.
CC       {ECO:0000256|HAMAP-Rule:MF_00913}.
CC   -!- SIMILARITY: Belongs to the SEDS family. FtsW subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00913}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000038; AAZ86892.1; -; Genomic_DNA.
DR   EnsemblBacteria; AAZ86892; AAZ86892; SSON_0097.
DR   KEGG; ssn:SSON_0097; -.
DR   HOGENOM; HOG000282689; -.
DR   KO; K03588; -.
DR   OMA; KGYQLSH; -.
DR   BioCyc; SSON300269:G1GL2-111-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000002529; 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; Q3Z5S0.
DR   SWISS-2DPAGE; Q3Z5S0.
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_00913};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_00913,
KW   ECO:0000313|EMBL:AAZ86892.1};
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00913};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00913,
KW   ECO:0000256|SAAS:SAAS00169496};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_00913,
KW   ECO:0000256|SAAS:SAAS00169500};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00913};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002529};
KW   Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_00913};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00913,
KW   ECO:0000256|SAAS:SAAS00176820};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00913};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00913};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_00913,
KW   ECO:0000256|SAAS:SAAS00176858};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00913,
KW   ECO:0000256|SAAS:SAAS00176861}.
FT   TRANSMEM     48     66       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00913}.
FT   TRANSMEM     87    104       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00913}.
FT   TRANSMEM    110    129       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00913}.
FT   TRANSMEM    175    192       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00913}.
FT   TRANSMEM    198    215       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00913}.
FT   TRANSMEM    222    239       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00913}.
FT   TRANSMEM    307    328       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00913}.
FT   TRANSMEM    340    364       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00913}.
FT   TRANSMEM    376    395       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00913}.
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
//

If you have problems or comments...

PBIL Back to PBIL home page