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SEPF_LACE2
ID   SEPF_LACE2              Reviewed;         183 AA.
AC   C4Z0N9;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Cell division protein SepF {ECO:0000255|HAMAP-Rule:MF_01197};
GN   Name=sepF {ECO:0000255|HAMAP-Rule:MF_01197};
GN   OrderedLocusNames=EUBELI_01152;
OS   Lachnospira eligens (strain ATCC 27750 / DSM 3376 / VPI C15-48 / C15-B4)
OS   (Eubacterium eligens).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Lachnospira.
OX   NCBI_TaxID=515620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27750 / DSM 3376 / VPI C15-48 / C15-B4;
RX   PubMed=19321416; DOI=10.1073/pnas.0901529106;
RA   Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S.,
RA   Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L.,
RA   Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C.,
RA   Hettich R.L., Gordon J.I.;
RT   "Characterizing a model human gut microbiota composed of members of its two
RT   dominant bacterial phyla.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009).
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; CP001104; ACR72152.1; -; Genomic_DNA.
DR   RefSeq; WP_012739387.1; NC_012778.1.
DR   AlphaFoldDB; C4Z0N9; -.
DR   SMR; C4Z0N9; -.
DR   STRING; 515620.EUBELI_01152; -.
DR   EnsemblBacteria; ACR72152; ACR72152; EUBELI_01152.
DR   GeneID; 41355876; -.
DR   KEGG; eel:EUBELI_01152; -.
DR   eggNOG; COG1799; Bacteria.
DR   HOGENOM; CLU_078499_4_0_9; -.
DR   OMA; KVGNGIF; -.
DR   OrthoDB; 2064885at2; -.
DR   Proteomes; UP000001476; 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..183
FT                   /note="Cell division protein SepF"
FT                   /id="PRO_1000213808"
FT   REGION          13..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..35
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..58
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   183 AA;  20536 MW;  0666E7F5642A6B14 CRC64;
     MGMLDGLTNM FKMHDDDDFD DDYEDYDDDF DEDYEDDKPS ARKRLFTGSS KKDSVADEEV
     SYTAEKPRFA SKSKVVPMKT QSARGLEVVV IRPESMEDAK EITDTLLTGK AVVLNLEGIH
     VEIAQRIIDY SAGSTYAIRG NLQKITNYIF LVTPPNVDIS GDIPEIVTGG IDLSSFNKNE
     NRF
 
 
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