ID   SEPF_STRMU              Reviewed;         191 AA.
AC   Q8DVD7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Cell division protein SepF {ECO:0000255|HAMAP-Rule:MF_01197};
GN   Name=sepF {ECO:0000255|HAMAP-Rule:MF_01197}; OrderedLocusNames=SMU_554;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA   Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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; AE014133; AAN58296.1; -; Genomic_DNA.
DR   RefSeq; NP_720990.1; NC_004350.2.
DR   RefSeq; WP_002262071.1; NC_004350.2.
DR   AlphaFoldDB; Q8DVD7; -.
DR   SMR; Q8DVD7; -.
DR   STRING; 210007.SMU_554; -.
DR   PRIDE; Q8DVD7; -.
DR   EnsemblBacteria; AAN58296; AAN58296; SMU_554.
DR   GeneID; 66817972; -.
DR   KEGG; smu:SMU_554; -.
DR   PATRIC; fig|210007.7.peg.489; -.
DR   eggNOG; COG1799; Bacteria.
DR   HOGENOM; CLU_078499_2_0_9; -.
DR   OMA; ASERHYQ; -.
DR   PhylomeDB; Q8DVD7; -.
DR   Proteomes; UP000002512; 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..191
FT                   /note="Cell division protein SepF"
FT                   /id="PRO_0000334095"
FT   REGION          21..96
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..74
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..95
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   191 AA;  21640 MW;  A1BE619A06D4D6C8 CRC64;
     MALRDSFNKI ISYFDTDEVS EVEEPAVASV KRQQDAAQPA SQQQKAQSHQ YHQSASRPSQ
     QQVQSGQNRR SGEENIHSLP TRRQSHNQQP AQEKTTIALK LPRKYEDAEE IVDLLIRNEC
     VLIDFQYMLE AQARRCLDFI DGASKVLAGN LQKVGASMYL LTPINVIVDA EEMTLAANGQ
     DVSFNYDMKR R