ID   SEPF_MYCMM              Reviewed;         223 AA.
AC   B2HGR0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Cell division protein SepF {ECO:0000255|HAMAP-Rule:MF_01197};
GN   Name=sepF {ECO:0000255|HAMAP-Rule:MF_01197}; OrderedLocusNames=MMAR_3187;
OS   Mycobacterium marinum (strain ATCC BAA-535 / M).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=216594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-535 / M;
RX   PubMed=18403782; DOI=10.1101/gr.075069.107;
RA   Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA   Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA   Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA   Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA   Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA   Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT   "Insights from the complete genome sequence of Mycobacterium marinum on the
RT   evolution of Mycobacterium tuberculosis.";
RL   Genome Res. 18:729-741(2008).
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; CP000854; ACC41613.1; -; Genomic_DNA.
DR   RefSeq; WP_012394853.1; NC_010612.1.
DR   AlphaFoldDB; B2HGR0; -.
DR   SMR; B2HGR0; -.
DR   STRING; 216594.MMAR_3187; -.
DR   EnsemblBacteria; ACC41613; ACC41613; MMAR_3187.
DR   GeneID; 64261849; -.
DR   KEGG; mmi:MMAR_3187; -.
DR   eggNOG; COG1799; Bacteria.
DR   HOGENOM; CLU_078499_0_0_11; -.
DR   OMA; YFGMVPL; -.
DR   OrthoDB; 2064885at2; -.
DR   Proteomes; UP000001190; 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..223
FT                   /note="Cell division protein SepF"
FT                   /id="PRO_1000138474"
FT   REGION          19..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..67
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   223 AA;  25702 MW;  C7F69037D127E74E CRC64;
     MSTLHKVKAY FGMAPMEDYD DEYYDDRGPS RGYSRPRFED DYGRYEGRDF EDPRRDPRAD
     MRADLRGEPA DYPPPGGYRG GYPDEARFQP REFDRADMAR PRFGSWLRNP TRGSLAMDPR
     RMAMMFEEGH PLSKITTLRP KDYSEARTIG ERFRDGTPVI MDLVSMDNAD AKRLVDFAAG
     LAFALRGSFD KVATKVFLLS PADVDVTPEE RRRIAETGFY AYQ