ID   SEPF_STRT2              Reviewed;         189 AA.
AC   Q5M4X6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, 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=stu0737;
OS   Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=264199;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-250 / LMG 18311;
RX   PubMed=15543133; DOI=10.1038/nbt1034;
RA   Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D.,
RA   Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., Fonstein M.,
RA   Overbeek R., Kyprides N., Purnelle B., Prozzi D., Ngui K., Masuy D.,
RA   Hancy F., Burteau S., Boutry M., Delcour J., Goffeau A., Hols P.;
RT   "Complete sequence and comparative genome analysis of the dairy bacterium
RT   Streptococcus thermophilus.";
RL   Nat. Biotechnol. 22:1554-1558(2004).
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; CP000023; AAV60430.1; -; Genomic_DNA.
DR   RefSeq; WP_011225780.1; NC_006448.1.
DR   AlphaFoldDB; Q5M4X6; -.
DR   SMR; Q5M4X6; -.
DR   STRING; 264199.stu0737; -.
DR   DNASU; 3164448; -.
DR   EnsemblBacteria; AAV60430; AAV60430; stu0737.
DR   GeneID; 66898636; -.
DR   KEGG; stl:stu0737; -.
DR   PATRIC; fig|264199.4.peg.744; -.
DR   eggNOG; COG1799; Bacteria.
DR   HOGENOM; CLU_078499_2_0_9; -.
DR   OMA; DVQKTQV; -.
DR   Proteomes; UP000001170; 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..189
FT                   /note="Cell division protein SepF"
FT                   /id="PRO_0000334112"
FT   REGION          18..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..34
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        35..49
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..64
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   189 AA;  21671 MW;  260DA263D0755AC5 CRC64;
     MAIKDAIEKI VSYFDADEVT DHEDVAKERP VKVQKTEQTP SQQQRKPERP QETVPPRRQH
     IKSDVQETQV LRSLSLSRSQ VNQGSQQMNT TKTTIAIKYP KKYEDAQEIV ELLIENECVL
     IDFQYMLEAQ ARRCLDFIDG ASKVLTGNLQ KVGSSMYLLT PINVVVDIEE IGLSHGNQES
     TFDFDMKRR