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Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7

DescriptionRecName: Full=Cell division protein SepF {ECO:0000255|HAMAP-Rule:MF_01197};
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MyHits synonymsSEPF_COPPD , B5Y7T0 , 3DA518E23A0FB439
match map segment
ipfam:SepF ihamap:SepF  
ID   SEPF_COPPD              Reviewed;         139 AA.
AC   B5Y7T0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   30-NOV-2016, entry version 48.
DE   RecName: Full=Cell division protein SepF {ECO:0000255|HAMAP-Rule:MF_01197};
GN   Name=sepF {ECO:0000255|HAMAP-Rule:MF_01197};
GN   OrderedLocusNames=COPRO5265_0466;
OS   Coprothermobacter proteolyticus (strain ATCC 35245 / DSM 5265 / BT).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermodesulfobiaceae; Coprothermobacter.
OX   NCBI_TaxID=309798;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35245 / DSM 5265 / BT;
RA   Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT   "The complete genome sequence of Coprothermobacter proteolyticus
RT   strain ATCC 5245 / DSM 5265 / BT.";
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cell division protein that is part of the divisome
CC       complex and is recruited early to the Z-ring. Probably stimulates
CC       Z-ring formation, perhaps through the cross-linking of FtsZ
CC       protofilaments. Its function overlaps with FtsA.
CC       {ECO:0000255|HAMAP-Rule:MF_01197}.
CC   -!- SUBUNIT: Homodimer. Interacts with FtsZ. {ECO:0000255|HAMAP-
CC       Rule:MF_01197}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01197}.
CC       Note=Localizes to the division site, in a FtsZ-dependent manner.
CC       {ECO:0000255|HAMAP-Rule:MF_01197}.
CC   -!- SIMILARITY: Belongs to the SepF family. {ECO:0000255|HAMAP-
CC       Rule:MF_01197}.
DR   EMBL; CP001145; ACI16784.1; -; Genomic_DNA.
DR   RefSeq; WP_012543436.1; NC_011295.1.
DR   STRING; 309798.COPRO5265_0466; -.
DR   EnsemblBacteria; ACI16784; ACI16784; COPRO5265_0466.
DR   KEGG; cpo:COPRO5265_0466; -.
DR   PATRIC; 21473782; VBICopPro72829_0443.
DR   eggNOG; ENOG4105VR5; Bacteria.
DR   eggNOG; COG1799; LUCA.
DR   KO; K09772; -.
DR   OrthoDB; POG091H029J; -.
DR   Proteomes; UP000001732; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0090529; P:cell septum assembly; IEA:UniProtKB-HAMAP.
DR   GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_01197; SepF; 1.
DR   InterPro; IPR023052; Cell_div_SepF.
DR   InterPro; IPR007561; Cell_div_SepF/SepF-rel.
DR   Pfam; PF04472; DUF552; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Complete proteome; Cytoplasm;
KW   Reference proteome; Septation.
FT   CHAIN         1    139       Cell division protein SepF.
FT                                /FTId=PRO_1000138465.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT        55    129       ipfam:SepF [T]
FT   MYHIT         4    137       ihamap:SepF [T]
SQ   SEQUENCE   139 AA;  15444 MW;  3DA518E23A0FB439 CRC64;
     MAEGGFWKKL TNFFTASEED EDIIEEDYMD EGYEAEEGTG FVPVQTRAVP VGSTIWVYQP
     SSFSFDVDSS FIGARIKDGY IIILNLQDLD DLSAQRLIDF VSGALYSVEG KLKAISSSVF
     LLVPKNVRVE SFNEGFGTE
//