SEPF2_STRCO
ID SEPF2_STRCO Reviewed; 213 AA.
AC Q9S2X2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Cell division protein SepF 2 {ECO:0000255|HAMAP-Rule:MF_01197};
GN Name=sepF2 {ECO:0000255|HAMAP-Rule:MF_01197}; OrderedLocusNames=SCO2079;
GN ORFNames=SC4A10.12c;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(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; AL939111; CAB51988.1; -; Genomic_DNA.
DR PIR; T34949; T34949.
DR RefSeq; NP_626338.1; NC_003888.3.
DR RefSeq; WP_003976736.1; NZ_VNID01000001.1.
DR AlphaFoldDB; Q9S2X2; -.
DR SMR; Q9S2X2; -.
DR STRING; 100226.SCO2079; -.
DR DNASU; 1097513; -.
DR GeneID; 1097513; -.
DR KEGG; sco:SCO2079; -.
DR PATRIC; fig|100226.15.peg.2112; -.
DR eggNOG; COG1799; Bacteria.
DR HOGENOM; CLU_078499_0_0_11; -.
DR InParanoid; Q9S2X2; -.
DR OMA; RKMAVYL; -.
DR PhylomeDB; Q9S2X2; -.
DR Proteomes; UP000001973; 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..213
FT /note="Cell division protein SepF 2"
FT /id="PRO_0000334119"
FT REGION 16..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..36
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..68
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 213 AA; 23723 MW; C26F7E31DFDD6D80 CRC64;
MAGAMRKMAV YLGLVEDDGY DGRGFDPDDD FEPELDPEPE RDHRRHEPAH QSHGAHQSQR
DEEVRVVQPP AQREPMPRAA SLAAESSRPA RIAPVASITQ ERASLEKSAP VIMPKVVSER
EPYRITTLHP RTYNEARTIG EHFREGTPVI MNLTEMDDTD AKRLVDFAAG LVFGLHGSIE
RVTQKVFLLS PANVDVTAED KARIAEGGFF NQS
