ID   SEPF_MYCLE              Reviewed;         210 AA.
AC   Q9CCE1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Cell division protein SepF {ECO:0000255|HAMAP-Rule:MF_01197};
GN   Name=sepF {ECO:0000255|HAMAP-Rule:MF_01197}; OrderedLocusNames=ML0920;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
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; AL583920; CAC31301.1; -; Genomic_DNA.
DR   PIR; B87024; B87024.
DR   RefSeq; NP_301703.1; NC_002677.1.
DR   RefSeq; WP_010908027.1; NC_002677.1.
DR   AlphaFoldDB; Q9CCE1; -.
DR   SMR; Q9CCE1; -.
DR   STRING; 272631.ML0920; -.
DR   EnsemblBacteria; CAC31301; CAC31301; CAC31301.
DR   KEGG; mle:ML0920; -.
DR   PATRIC; fig|272631.5.peg.1663; -.
DR   Leproma; ML0920; -.
DR   eggNOG; COG1799; Bacteria.
DR   HOGENOM; CLU_078499_0_0_11; -.
DR   OMA; YFGMVPL; -.
DR   Proteomes; UP000000806; 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..210
FT                   /note="Cell division protein SepF"
FT                   /id="PRO_0000334041"
SQ   SEQUENCE   210 AA;  24016 MW;  39CFFC949CE87FEB CRC64;
     MSTLHKVKAY FGMAPMEDYD DEYYDDRSPT HGYGRSRFEE GYGRYEGRDY SDLRGDPTGY
     LPLGYRGGYG DEHRFRPREF DRPDLSRPRL GSWLRNSTRG ALAMDPRRMA MLFDEGSPLS
     KITTLRPKDY SEARTIGERF RDGTPVIIDL VSMDNADAKR LVDFAAGLAF ALRGSFDKVA
     TKVFLLSPAD VDVSPEERRR IAETGFYAYQ