ID   SCPB_CLOBK              Reviewed;         193 AA.
AC   B1IMC4;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Segregation and condensation protein B {ECO:0000255|HAMAP-Rule:MF_01804};
GN   Name=scpB {ECO:0000255|HAMAP-Rule:MF_01804}; OrderedLocusNames=CLD_2784;
OS   Clostridium botulinum (strain Okra / Type B1).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=498213;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Okra / Type B1;
RX   PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA   Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA   Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT   "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT   and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT   plasmids.";
RL   PLoS ONE 2:E1271-E1271(2007).
CC   -!- FUNCTION: Participates in chromosomal partition during cell division.
CC       May act via the formation of a condensin-like complex containing Smc
CC       and ScpA that pull DNA away from mid-cell into both cell halves.
CC       {ECO:0000255|HAMAP-Rule:MF_01804}.
CC   -!- SUBUNIT: Homodimer. Homodimerization may be required to stabilize the
CC       binding of ScpA to the Smc head domains. Component of a cohesin-like
CC       complex composed of ScpA, ScpB and the Smc homodimer, in which ScpA and
CC       ScpB bind to the head domain of Smc. The presence of the three proteins
CC       is required for the association of the complex with DNA.
CC       {ECO:0000255|HAMAP-Rule:MF_01804}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01804}.
CC       Note=Associated with two foci at the outer edges of the nucleoid region
CC       in young cells, and at four foci within both cell halves in older
CC       cells. {ECO:0000255|HAMAP-Rule:MF_01804}.
CC   -!- SIMILARITY: Belongs to the ScpB family. {ECO:0000255|HAMAP-
CC       Rule:MF_01804}.
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DR   EMBL; CP000939; ACA43863.1; -; Genomic_DNA.
DR   RefSeq; WP_003402814.1; NC_010516.1.
DR   AlphaFoldDB; B1IMC4; -.
DR   SMR; B1IMC4; -.
DR   EnsemblBacteria; ACA43863; ACA43863; CLD_2784.
DR   GeneID; 5186111; -.
DR   KEGG; cbb:CLD_2784; -.
DR   HOGENOM; CLU_045647_5_3_9; -.
DR   OMA; DGWRFYT; -.
DR   Proteomes; UP000008541; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0051304; P:chromosome separation; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.10.10; -; 2.
DR   HAMAP; MF_01804; ScpB; 1.
DR   InterPro; IPR005234; ScpB_csome_segregation.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR34298; PTHR34298; 1.
DR   Pfam; PF04079; SMC_ScpB; 1.
DR   PIRSF; PIRSF019345; ScpB; 1.
DR   SUPFAM; SSF46785; SSF46785; 2.
DR   TIGRFAMs; TIGR00281; TIGR00281; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Chromosome partition; Cytoplasm.
FT   CHAIN           1..193
FT                   /note="Segregation and condensation protein B"
FT                   /id="PRO_1000187534"
SQ   SEQUENCE   193 AA;  21982 MW;  2D25A3FAAFA2A097 CRC64;
     MNKDHEEQLE INEVSQKNKY KSIIESLLFM SGEPINIKDL ATILNCKQDK VSSLLNEMNN
     SYVGKDRGIK ILIHNRAVQL VTKPENSIYV EKLLKTNVRQ SLSQAALETL SIIAYKQPIT
     RVAIDEIRGV KSDRAIYTLL EKNIIKECGR LDVPGKPILY GTTEEFLKFF GLDSIEAIPN
     LEDLLKEFSK EEN