SEPF_CUTAK
ID SEPF_CUTAK Reviewed; 172 AA.
AC Q6A9P7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Cell division protein SepF {ECO:0000255|HAMAP-Rule:MF_01197};
GN Name=sepF {ECO:0000255|HAMAP-Rule:MF_01197}; OrderedLocusNames=PPA0763;
OS Cutibacterium acnes (strain DSM 16379 / KPA171202) (Propionibacterium
OS acnes).
OC Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC Cutibacterium.
OX NCBI_TaxID=267747;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16379 / KPA171202;
RX PubMed=15286373; DOI=10.1126/science.1100330;
RA Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A.,
RA Strittmatter A., Hujer S., Duerre P., Gottschalk G.;
RT "The complete genome sequence of Propionibacterium acnes, a commensal of
RT human skin.";
RL Science 305:671-673(2004).
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; AE017283; AAT82519.1; -; Genomic_DNA.
DR RefSeq; WP_002530972.1; NZ_CP025935.1.
DR AlphaFoldDB; Q6A9P7; -.
DR SMR; Q6A9P7; -.
DR STRING; 267747.PPA0763; -.
DR EnsemblBacteria; AAT82519; AAT82519; PPA0763.
DR KEGG; pac:PPA0763; -.
DR PATRIC; fig|267747.3.peg.800; -.
DR eggNOG; COG1799; Bacteria.
DR HOGENOM; CLU_078499_0_0_11; -.
DR OMA; LTIMDPD; -.
DR Proteomes; UP000000603; 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..172
FT /note="Cell division protein SepF"
FT /id="PRO_0000334067"
FT REGION 18..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..35
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 172 AA; 19464 MW; A8DDC68D286CBEF4 CRC64;
MAGIGRKIAS YVGIVDDRRY DEEDLPDEEL TTEVYSDDGY EPSSEVTQLH HHDSNEQHAR
GHKAVQHRRR SELEEPSIAD INRILTVHPR NYNEARTIGE QFREGIPVIM NLTEMDDADA
KRLVDFAAGL IFGLRGTIER VTSKVFLLCP RNVNVTPEDK ARIASGGFFN QS