SEPF_STRPF
ID SEPF_STRPF Reviewed; 218 AA.
AC Q1J5T2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Cell division protein SepF {ECO:0000255|HAMAP-Rule:MF_01197};
GN Name=sepF {ECO:0000255|HAMAP-Rule:MF_01197};
GN OrderedLocusNames=MGAS10750_Spy1354;
OS Streptococcus pyogenes serotype M4 (strain MGAS10750).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=370554;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGAS10750;
RX PubMed=16636287; DOI=10.1073/pnas.0510279103;
RA Beres S.B., Richter E.W., Nagiec M.J., Sumby P., Porcella S.F., DeLeo F.R.,
RA Musser J.M.;
RT "Molecular genetic anatomy of inter- and intraserotype variation in the
RT human bacterial pathogen group A Streptococcus.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7059-7064(2006).
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=ABF38304.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000262; ABF38304.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_021299320.1; NC_008024.1.
DR AlphaFoldDB; Q1J5T2; -.
DR SMR; Q1J5T2; -.
DR EnsemblBacteria; ABF38304; ABF38304; MGAS10750_Spy1354.
DR KEGG; spi:MGAS10750_Spy1354; -.
DR HOGENOM; CLU_078499_2_0_9; -.
DR Proteomes; UP000002434; 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..218
FT /note="Cell division protein SepF"
FT /id="PRO_0000334106"
FT REGION 24..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 218 AA; 25249 MW; F91CFB450F9F2F70 CRC64;
MAFKDTFNKM ISYFDTDEVN EVEEDVTAST DNVIPRSQQS VRASSHPKQE PRNNHVQQDH
QARSQEQTRS QMHPKHGTSE RYYQQSQPKE GHEMVDRRKR MSTSGIANRR EQYQQSTCSD
QTTIALKYPR KYEDAQEIVD LLIVNECVLI DFQFMLDAQA RRCLDFIDGA SKVLYGSLQK
VGSSMYLLAP SNVSVNIEEM TIPHTTQDIG FDFDMKRR