ID   SEPF_BACCR              Reviewed;         156 AA.
AC   Q812W8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Cell division protein SepF {ECO:0000255|HAMAP-Rule:MF_01197};
GN   Name=sepF {ECO:0000255|HAMAP-Rule:MF_01197}; OrderedLocusNames=BC_3899;
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS   15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC   / NCTC 2599 / NRRL B-3711;
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA   Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA   Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA   Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT   anthracis.";
RL   Nature 423:87-91(2003).
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; AE016877; AAP10820.1; -; Genomic_DNA.
DR   RefSeq; NP_833619.1; NC_004722.1.
DR   RefSeq; WP_000119129.1; NZ_CP034551.1.
DR   AlphaFoldDB; Q812W8; -.
DR   SMR; Q812W8; -.
DR   STRING; 226900.BC_3899; -.
DR   EnsemblBacteria; AAP10820; AAP10820; BC_3899.
DR   GeneID; 67508533; -.
DR   KEGG; bce:BC3899; -.
DR   PATRIC; fig|226900.8.peg.4021; -.
DR   HOGENOM; CLU_078499_4_1_9; -.
DR   OMA; KVGNGIF; -.
DR   Proteomes; UP000001417; 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..156
FT                   /note="Cell division protein SepF"
FT                   /id="PRO_0000333977"
FT   REGION          20..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..37
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   156 AA;  17723 MW;  F30B5A0CF5E32FBF CRC64;
     MSWSKVKYFF FDTPEEKEAA QYGYEKEQTD MKKQQDPPEQ QDVTFPKAQP KQNVVSIETA
     KQSSKVVLLE PRTYSEAQGI ADHLKGRRAV VINLQRMSTD QAVRIVDFLS GTVYAIGGDI
     QKIGPKTFMC TPENVDIVGA ISELFGEEEE TNIKRW