SEPF_RHOE4
ID SEPF_RHOE4 Reviewed; 216 AA.
AC C1A0W9;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=Cell division protein SepF {ECO:0000255|HAMAP-Rule:MF_01197};
GN Name=sepF {ECO:0000255|HAMAP-Rule:MF_01197}; OrderedLocusNames=RER_35460;
OS Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus;
OC Rhodococcus erythropolis group.
OX NCBI_TaxID=234621;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PR4 / NBRC 100887;
RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT PR4 and Rhodococcus opacus B4.";
RL Submitted (MAR-2005) 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; AP008957; BAH34254.1; -; Genomic_DNA.
DR RefSeq; WP_003941752.1; NC_012490.1.
DR AlphaFoldDB; C1A0W9; -.
DR SMR; C1A0W9; -.
DR STRING; 234621.RER_35460; -.
DR EnsemblBacteria; BAH34254; BAH34254; RER_35460.
DR GeneID; 64141335; -.
DR KEGG; rer:RER_35460; -.
DR eggNOG; COG1799; Bacteria.
DR HOGENOM; CLU_078499_0_0_11; -.
DR OMA; YFGMVPL; -.
DR Proteomes; UP000002204; 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; Septation.
FT CHAIN 1..216
FT /note="Cell division protein SepF"
FT /id="PRO_1000213814"
FT REGION 22..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 216 AA; 24325 MW; 65CC5ACABBAED966 CRC64;
MSNLHKFKAY FGMVPLDDYE DEYVEEPDQA RRAPRRSHDG YAERDDREFV EPAFSKASYA
PSRRDEEDAE FDRYDSRPRV DTVPSRSSRP AMAPRPASRG NLAVDARAER PEARRAPVVD
DGGPLAKITT LRPQSYAEAR TIGERFRDGT PVIMDLVDMS NADAKRLVDF AAGLAFALRG
SFDKVATKVF LLSPADIDVS AEERRRIAET GFYSQK