ID   SEPF_SYNE7              Reviewed;         191 AA.
AC   Q31LI0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Cell division protein SepF {ECO:0000255|HAMAP-Rule:MF_01197};
GN   Name=sepF {ECO:0000255|HAMAP-Rule:MF_01197};
GN   OrderedLocusNames=Synpcc7942_2059;
OS   Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS   R2).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX   NCBI_TaxID=1140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7942 / FACHB-805;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION IN CELL DIVISION.
RX   PubMed=15773984; DOI=10.1111/j.1365-2958.2005.04548.x;
RA   Miyagishima S.Y., Wolk C.P., Osteryoung K.W.;
RT   "Identification of cyanobacterial cell division genes by comparative and
RT   mutational analyses.";
RL   Mol. Microbiol. 56:126-143(2005).
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       ECO:0000269|PubMed:15773984}.
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; CP000100; ABB58089.1; -; Genomic_DNA.
DR   RefSeq; WP_011378295.1; NC_007604.1.
DR   AlphaFoldDB; Q31LI0; -.
DR   SMR; Q31LI0; -.
DR   STRING; 1140.Synpcc7942_2059; -.
DR   PRIDE; Q31LI0; -.
DR   EnsemblBacteria; ABB58089; ABB58089; Synpcc7942_2059.
DR   KEGG; syf:Synpcc7942_2059; -.
DR   eggNOG; COG1799; Bacteria.
DR   HOGENOM; CLU_078499_1_0_3; -.
DR   OMA; PAWGTDS; -.
DR   OrthoDB; 2064885at2; -.
DR   BioCyc; SYNEL:SYNPCC7942_2059-MON; -.
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   1: Evidence at protein level;
KW   Cell cycle; Cell division; Cytoplasm; Septation.
FT   CHAIN           1..191
FT                   /note="Cell division protein SepF"
FT                   /id="PRO_0000334128"
FT   REGION          157..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..184
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   191 AA;  21004 MW;  17CCB3F1AC58C0F2 CRC64;
     MSFVNRIRDI VGLNESLDYD EEYETYDVAA DSYNGYNDAA ETSSRRRQRN HTPTASIEPV
     STASNVIGLP GLSSSSEVVV MEPRSFEEMP QAIQALRERK TIVLNLTMME PDQAQRAVDF
     VAGGTFAIDG HQERVGESIF LFTPSCVHVT TQGGEQYLNE SPAQPVQTTT SFGRTATPTP
     AWGTDSRYAA Q