ID   SEPF_CYAP4              Reviewed;         210 AA.
AC   B8HPI0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=Cell division protein SepF {ECO:0000255|HAMAP-Rule:MF_01197};
GN   Name=sepF {ECO:0000255|HAMAP-Rule:MF_01197};
GN   OrderedLocusNames=Cyan7425_1471;
OS   Cyanothece sp. (strain PCC 7425 / ATCC 29141).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC   Cyanothecaceae; Cyanothece; unclassified Cyanothece.
OX   NCBI_TaxID=395961;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7425 / ATCC 29141;
RX   PubMed=21972240; DOI=10.1128/mbio.00214-11;
RA   Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H.,
RA   Sherman L.A., Pakrasi H.B.;
RT   "Novel metabolic attributes of the genus Cyanothece, comprising a group of
RT   unicellular nitrogen-fixing Cyanobacteria.";
RL   MBio 2:E214-E214(2011).
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}.
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; CP001344; ACL43841.1; -; Genomic_DNA.
DR   RefSeq; WP_012626932.1; NC_011884.1.
DR   AlphaFoldDB; B8HPI0; -.
DR   SMR; B8HPI0; -.
DR   STRING; 395961.Cyan7425_1471; -.
DR   EnsemblBacteria; ACL43841; ACL43841; Cyan7425_1471.
DR   KEGG; cyn:Cyan7425_1471; -.
DR   eggNOG; COG1799; Bacteria.
DR   HOGENOM; CLU_078499_1_1_3; -.
DR   OMA; LTIMDPD; -.
DR   OrthoDB; 2064885at2; -.
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; Septation.
FT   CHAIN           1..210
FT                   /note="Cell division protein SepF"
FT                   /id="PRO_1000164534"
FT   REGION          13..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..78
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   210 AA;  23200 MW;  83A350F5E8DA8F12 CRC64;
     MSSIFGKLRE FVGFGEPTGY DYDYDEMEGD DYQGLYPAEP AQSLPTRSEE PHPRPSEPEM
     RSPVNTSAVT STAMNPPMNQ SMNNVVGMPG SGKWWGAVAE VIVMEPRSFE EMPQVIQALR
     ERKSVVLNLT MMEPDQAQRA VDFVAGATYT IDGHQERIGE SIFLFTPSCV QVSTQAGGQS
     HTLRDIPQAQ IHTRPPAPAW TAEPLSRIAQ