ID   SEPF_LACLM              Reviewed;         196 AA.
AC   Q9ZAI9; A2RMT9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-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=llmg_2058;
OS   Lactococcus lactis subsp. cremoris (strain MG1363).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus; Lactococcus cremoris subsp. cremoris.
OX   NCBI_TaxID=416870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Sorensen K.I., Vogensen F.K., Hammer K.;
RT   "Cloning and characterization of a cell division operon in Lactococcus
RT   lactis strain MG1363.";
RL   Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MG1363;
RX   PubMed=17307855; DOI=10.1128/jb.01768-06;
RA   Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA   Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA   van Sinderen D., Kok J.;
RT   "The complete genome sequence of the lactic acid bacterial paradigm
RT   Lactococcus lactis subsp. cremoris MG1363.";
RL   J. Bacteriol. 189:3256-3270(2007).
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; Y15422; CAA75618.1; -; Genomic_DNA.
DR   EMBL; AM406671; CAL98625.1; -; Genomic_DNA.
DR   RefSeq; WP_011835772.1; NZ_WJVF01000004.1.
DR   AlphaFoldDB; Q9ZAI9; -.
DR   SMR; Q9ZAI9; -.
DR   STRING; 416870.llmg_2058; -.
DR   EnsemblBacteria; CAL98625; CAL98625; llmg_2058.
DR   KEGG; llm:llmg_2058; -.
DR   eggNOG; COG1799; Bacteria.
DR   HOGENOM; CLU_078499_2_0_9; -.
DR   OMA; ASERHYQ; -.
DR   PhylomeDB; Q9ZAI9; -.
DR   BioCyc; LLAC416870:LLMG_RS10275-MON; -.
DR   Proteomes; UP000000364; 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; Septation.
FT   CHAIN           1..196
FT                   /note="Cell division protein SepF"
FT                   /id="PRO_0000334027"
FT   REGION          15..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..80
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   196 AA;  21938 MW;  BB4E472D05A699B2 CRC64;
     MAFKDWMNNL RDYFVEDDEE FNEPTRPVQE SRPTVASTPK PKVEERKVQA DYQSRRPAQT
     TPKPQTQTAA PKRSASTFSK PMPEKIVQQQ TVSQAQSLAA TVSTIAIKEP RAYADIMESA
     RIVKNGECVL VNFKFMGDAQ ARRSIDFMTG VVFTLDGDIQ NVGGQIFLMT PANITVDAAK
     EMSILAGQNF ESYDIY