ID   SEPF_SALAI              Reviewed;         226 AA.
AC   A8LX76;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Cell division protein SepF {ECO:0000255|HAMAP-Rule:MF_01197};
GN   Name=sepF {ECO:0000255|HAMAP-Rule:MF_01197}; OrderedLocusNames=Sare_3434;
OS   Salinispora arenicola (strain CNS-205).
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   Salinispora.
OX   NCBI_TaxID=391037;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNS-205;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Foster B., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Jensen P.R., Moore B.S., Penn K., Jenkins C.,
RA   Udwary D., Xiang L., Gontang E., Richardson P.;
RT   "Complete sequence of Salinispora arenicola CNS-205.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000850; ABV99236.1; -; Genomic_DNA.
DR   RefSeq; WP_012183528.1; NC_009953.1.
DR   AlphaFoldDB; A8LX76; -.
DR   SMR; A8LX76; -.
DR   STRING; 391037.Sare_3434; -.
DR   EnsemblBacteria; ABV99236; ABV99236; Sare_3434.
DR   GeneID; 5704115; -.
DR   KEGG; saq:Sare_3434; -.
DR   PATRIC; fig|391037.6.peg.3461; -.
DR   eggNOG; COG1799; Bacteria.
DR   HOGENOM; CLU_078499_0_0_11; -.
DR   OMA; STHANER; -.
DR   OrthoDB; 2064885at2; -.
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..226
FT                   /note="Cell division protein SepF"
FT                   /id="PRO_0000334072"
FT   REGION          20..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..45
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        56..97
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        99..115
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   226 AA;  25408 MW;  28A46EDB5450369E CRC64;
     MGALRKAGVW LGLVEEDDER AYDDAGYDKG GYRESRYRSS RYSEDFGDED DEDEEAAVPR
     SRRGDRSRLE RAAARSGDVD HNVEGEQPER VERASVRSIT RSAEPSESLT YHTRDNLALA
     PQPVRERVPA DEEQRYQITT LHPTTYREAR TIGEHFRDGV PVIINLTEMD EADARRLVDF
     AAGLAFGLRG TIERVTNRVF LLSPANVQVT AEDKAKIAEG GFFSLS