SEPF_BACSU
ID SEPF_BACSU Reviewed; 151 AA.
AC O31728;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 3.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Cell division protein SepF;
GN Name=sepF; Synonyms=ylmF; OrderedLocusNames=BSU15390;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP SEQUENCE REVISION TO 5; 31 AND 88.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [3]
RP FUNCTION IN CELL DIVISION, AND SUBCELLULAR LOCATION.
RC STRAIN=168;
RX PubMed=16420366; DOI=10.1111/j.1365-2958.2005.04987.x;
RA Hamoen L.W., Meile J.-C., de Jong W., Noirot P., Errington J.;
RT "SepF, a novel FtsZ-interacting protein required for a late step in cell
RT division.";
RL Mol. Microbiol. 59:989-999(2006).
RN [4]
RP FUNCTION IN CELL DIVISION, SUBCELLULAR LOCATION, SUBUNIT, AND INTERACTION
RP WITH FTSZ.
RC STRAIN=168;
RX PubMed=16796675; DOI=10.1111/j.1365-2958.2006.05184.x;
RA Ishikawa S., Kawai Y., Hiramatsu K., Kuwano M., Ogasawara N.;
RT "A new FtsZ-interacting protein, YlmF, complements the activity of FtsA
RT during progression of cell division in Bacillus subtilis.";
RL Mol. Microbiol. 60:1364-1380(2006).
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:0000269|PubMed:16420366,
CC ECO:0000269|PubMed:16796675}.
CC -!- SUBUNIT: Homodimer. Interacts with FtsZ. {ECO:0000269|PubMed:16796675}.
CC -!- INTERACTION:
CC O31728; P17865: ftsZ; NbExp=8; IntAct=EBI-2122748, EBI-1569853;
CC O31728; O31728: sepF; NbExp=4; IntAct=EBI-2122748, EBI-2122748;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16420366,
CC ECO:0000269|PubMed:16796675}. Note=Localizes to the division site, in a
CC FtsZ-dependent manner.
CC -!- SIMILARITY: Belongs to the SepF family. {ECO:0000305}.
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DR EMBL; AL009126; CAB13413.3; -; Genomic_DNA.
DR PIR; F69876; F69876.
DR RefSeq; NP_389422.2; NC_000964.3.
DR RefSeq; WP_003244791.1; NZ_CP053102.1.
DR PDB; 3ZIH; X-ray; 2.00 A; A/B=57-151.
DR PDB; 3ZII; X-ray; 2.20 A; A=57-151.
DR PDBsum; 3ZIH; -.
DR PDBsum; 3ZII; -.
DR AlphaFoldDB; O31728; -.
DR SMR; O31728; -.
DR IntAct; O31728; 4.
DR MINT; O31728; -.
DR STRING; 224308.BSU15390; -.
DR jPOST; O31728; -.
DR PaxDb; O31728; -.
DR PRIDE; O31728; -.
DR EnsemblBacteria; CAB13413; CAB13413; BSU_15390.
DR GeneID; 939952; -.
DR KEGG; bsu:BSU15390; -.
DR PATRIC; fig|224308.179.peg.1677; -.
DR eggNOG; COG1799; Bacteria.
DR InParanoid; O31728; -.
DR OMA; KVGNGIF; -.
DR BioCyc; BSUB:BSU15390-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0090529; P:cell septum assembly; IMP:CACAO.
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 3D-structure; Cell cycle; Cell division; Cytoplasm; Reference proteome;
KW Septation.
FT CHAIN 1..151
FT /note="Cell division protein SepF"
FT /id="PRO_0000333984"
FT REGION 23..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:3ZIH"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:3ZIH"
FT HELIX 75..83
FT /evidence="ECO:0007829|PDB:3ZIH"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:3ZIH"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:3ZIH"
FT HELIX 97..114
FT /evidence="ECO:0007829|PDB:3ZIH"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:3ZIH"
FT STRAND 125..129
FT /evidence="ECO:0007829|PDB:3ZIH"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:3ZIH"
SQ SEQUENCE 151 AA; 17386 MW; 17D90E9526FC4A07 CRC64;
MSMKNKLKNF FSMEDEEYEY EYIETERESH EEHEQKEKPA YNGNKPAGKQ NVVSLQSVQK
SSKVVLSEPR VYAEAQEIAD HLKNRRAVVV NLQRIQHDQA KRIVDFLSGT VYAIGGDIQR
IGSDIFLCTP DNVDVSGTIS ELISEDEHQR W
