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SEPF_THEFY
ID   SEPF_THEFY              Reviewed;         173 AA.
AC   Q47QW3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   25-MAY-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=Tfu_1116;
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX;
RX   PubMed=17209016; DOI=10.1128/jb.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M., DiBartolo G.,
RA   Martinez M., Lapidus A., Lucas S., Copeland A., Richardson P., Wilson D.B.,
RA   Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAZ55154.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000088; AAZ55154.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_038043538.1; NC_007333.1.
DR   AlphaFoldDB; Q47QW3; -.
DR   SMR; Q47QW3; -.
DR   STRING; 269800.Tfu_1116; -.
DR   EnsemblBacteria; AAZ55154; AAZ55154; Tfu_1116.
DR   KEGG; tfu:Tfu_1116; -.
DR   eggNOG; COG1799; Bacteria.
DR   HOGENOM; CLU_078499_0_0_11; -.
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..173
FT                   /note="Cell division protein SepF"
FT                   /id="PRO_0000334134"
FT   REGION          31..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..69
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   173 AA;  19540 MW;  40C9EBC1EC7A1F32 CRC64;
     MAGALRKMAV YLGLVEDDRY DHRYADEYDD FEDFDEPLDE RPSRNRSPRD DSRNNAVTDS
     SDHSPSRNER RSPAPAPATA DLARITTLHP RTYNEARTIG EHFREGIPVI MNLTEMVDSD
     AKRLVDFAAG LIFGLHGSIE RVTNKVFLLS PANVEVTAED KARIAERGFF NQS
 
 
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