SEPF_STRA5
ID SEPF_STRA5 Reviewed; 201 AA.
AC Q8E181;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Cell division protein SepF {ECO:0000255|HAMAP-Rule:MF_01197};
GN Name=sepF {ECO:0000255|HAMAP-Rule:MF_01197}; OrderedLocusNames=SAG0481;
OS Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=208435;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-611 / 2603 V/R;
RX PubMed=12200547; DOI=10.1073/pnas.182380799;
RA Tettelin H., Masignani V., Cieslewicz M.J., Eisen J.A., Peterson S.N.,
RA Wessels M.R., Paulsen I.T., Nelson K.E., Margarit I., Read T.D.,
RA Madoff L.C., Wolf A.M., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Lewis M.R., Radune D.,
RA Fedorova N.B., Scanlan D., Khouri H.M., Mulligan S., Carty H.A.,
RA Cline R.T., Van Aken S.E., Gill J., Scarselli M., Mora M., Iacobini E.T.,
RA Brettoni C., Galli G., Mariani M., Vegni F., Maione D., Rinaudo D.,
RA Rappuoli R., Telford J.L., Kasper D.L., Grandi G., Fraser C.M.;
RT "Complete genome sequence and comparative genomic analysis of an emerging
RT human pathogen, serotype V Streptococcus agalactiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(2002).
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; AE009948; AAM99383.1; -; Genomic_DNA.
DR RefSeq; NP_687511.1; NC_004116.1.
DR RefSeq; WP_001185366.1; NC_004116.1.
DR AlphaFoldDB; Q8E181; -.
DR SMR; Q8E181; -.
DR STRING; 208435.SAG0481; -.
DR EnsemblBacteria; AAM99383; AAM99383; SAG0481.
DR KEGG; sag:SAG0481; -.
DR PATRIC; fig|208435.3.peg.479; -.
DR HOGENOM; CLU_078499_2_0_9; -.
DR OMA; ASERHYQ; -.
DR Proteomes; UP000000821; 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..201
FT /note="Cell division protein SepF"
FT /id="PRO_0000334093"
FT REGION 27..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 201 AA; 23463 MW; 68252098334AF9E2 CRC64;
MALKDRFDKI ISYFDTDDVS ENEVHEVQER TSVQRDSRAA TAQEASQRSH MTNSAEEEMI
GSRPRTYTYD PNRQERQRVQ RDNAYQQATP RVQNKDSVRQ QREQVTIALK YPRKYEDAQE
IVDLLIVNEC VLIDFQYMLD AQARRCLDYI DGASRVLYGS LQKVGSSMFL LTPANVMVDI
EEMNIPKTGQ ETSFDFDMKR R