(data stored in SCRATCH zone)

SWISSPROT: B7UID9_ECO27

ID   B7UID9_ECO27            Unreviewed;       414 AA.
AC   B7UID9;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 64.
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:CAS07642.1};
GN   OrderedLocusNames=E2348C_0094 {ECO:0000313|EMBL:CAS07642.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS07642.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS07642.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
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; FM180568; CAS07642.1; -; Genomic_DNA.
DR   RefSeq; WP_001356870.1; NC_011601.1.
DR   EnsemblBacteria; CAS07642; CAS07642; E2348C_0094.
DR   KEGG; ecg:E2348C_0094; -.
DR   HOGENOM; HOG000282689; -.
DR   KO; K03588; -.
DR   OMA; KGYQLSH; -.
DR   BioCyc; ECOL574521:E2348C_RS00485-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000008205; 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; B7UID9.
DR   SWISS-2DPAGE; B7UID9.
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_00913};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_00913,
KW   ECO:0000313|EMBL:CAS07642.1};
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:UP000008205};
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;  45986 MW;  E6510C9788DFE3F2 CRC64;
     MRLSLPRLKM PRLPGFSILV WISTALKGWV MGSREKDTNS 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