SEPF_CLOD6
ID SEPF_CLOD6 Reviewed; 152 AA.
AC Q182V6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Cell division protein SepF {ECO:0000255|HAMAP-Rule:MF_01197};
GN Name=sepF {ECO:0000255|HAMAP-Rule:MF_01197}; OrderedLocusNames=CD630_26220;
OS Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Clostridioides.
OX NCBI_TaxID=272563;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=630;
RX PubMed=16804543; DOI=10.1038/ng1830;
RA Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., Unwin L.,
RA Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT mobile, mosaic genome.";
RL Nat. Genet. 38:779-786(2006).
CC -!- FUNCTION: Cell division protein that is part of the divisome complex
CC and is recruited early to the Z-ring. Probably stimulates Z-ring
CC formation, perhaps through the cross-linking of FtsZ protofilaments.
CC Its function overlaps with FtsA. {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}.
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DR EMBL; AM180355; CAJ69508.1; -; Genomic_DNA.
DR RefSeq; WP_003416162.1; NZ_CP010905.2.
DR RefSeq; YP_001089133.1; NC_009089.1.
DR AlphaFoldDB; Q182V6; -.
DR SMR; Q182V6; -.
DR STRING; 272563.CD630_26220; -.
DR EnsemblBacteria; CAJ69508; CAJ69508; CD630_26220.
DR GeneID; 66355020; -.
DR KEGG; cdf:CD630_26220; -.
DR KEGG; pdc:CDIF630_02876; -.
DR PATRIC; fig|272563.120.peg.2765; -.
DR eggNOG; COG1799; Bacteria.
DR OMA; KVGNGIF; -.
DR PhylomeDB; Q182V6; -.
DR BioCyc; PDIF272563:G12WB-2773-MON; -.
DR Proteomes; UP000001978; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.110.150; -; 1.
DR HAMAP; MF_01197; SepF; 1.
DR InterPro; IPR023052; Cell_div_SepF.
DR InterPro; IPR007561; Cell_div_SepF/SepF-rel.
DR InterPro; IPR038594; SepF-like_sf.
DR PANTHER; PTHR35798; PTHR35798; 1.
DR Pfam; PF04472; SepF; 1.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Cytoplasm; Reference proteome; Septation.
FT CHAIN 1..152
FT /note="Cell division protein SepF"
FT /id="PRO_0000333997"
SQ SEQUENCE 152 AA; 17269 MW; 89D7A1C1B801603A CRC64;
MSNGIISKFK NWIVDEEEDY IEDEYESGMD DIVQEEEMNS GFSTAKANKI VNLHTTSQMK
VVIVEPKVYD EAATIADHLK QRRAVIVNLE GLTNSEVRKS IFNFMNGAVY VLDGSIQKVS
KSIFILAPNN VDIDANMKKE LESKAFFPWQ NK