ID   SCPB_SYMTH              Reviewed;         219 AA.
AC   Q67NF6;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Segregation and condensation protein B {ECO:0000255|HAMAP-Rule:MF_01804};
GN   Name=scpB {ECO:0000255|HAMAP-Rule:MF_01804}; OrderedLocusNames=STH1802;
OS   Symbiobacterium thermophilum (strain T / IAM 14863).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Symbiobacteriaceae;
OC   Symbiobacterium.
OX   NCBI_TaxID=292459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T / IAM 14863;
RX   PubMed=15383646; DOI=10.1093/nar/gkh830;
RA   Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K.,
RA   Ikeda H., Hattori M., Beppu T.;
RT   "Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium
RT   that depends on microbial commensalism.";
RL   Nucleic Acids Res. 32:4937-4944(2004).
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; AP006840; BAD40787.1; -; Genomic_DNA.
DR   RefSeq; WP_011195930.1; NC_006177.1.
DR   AlphaFoldDB; Q67NF6; -.
DR   SMR; Q67NF6; -.
DR   STRING; 292459.STH1802; -.
DR   PRIDE; Q67NF6; -.
DR   EnsemblBacteria; BAD40787; BAD40787; STH1802.
DR   KEGG; sth:STH1802; -.
DR   eggNOG; COG1386; Bacteria.
DR   HOGENOM; CLU_045647_5_2_9; -.
DR   OMA; DGWRFYT; -.
DR   OrthoDB; 1771906at2; -.
DR   Proteomes; UP000000417; 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   SUPFAM; SSF46785; SSF46785; 2.
DR   TIGRFAMs; TIGR00281; TIGR00281; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Chromosome partition; Cytoplasm;
KW   Reference proteome.
FT   CHAIN           1..219
FT                   /note="Segregation and condensation protein B"
FT                   /id="PRO_0000273316"
FT   REGION          193..219
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   219 AA;  23850 MW;  1A53B420DFBB727C CRC64;
     MIWNHGKMIL EALLLASPEP LTIKRIAEVI GLDERDAALL MADLQKDYEA PHRGLAIREM
     AGGYVLTTRP EAAEYVERLL QPKSRGLSHA ALETLAIIAY RQPITKAEIE NVRGVKVDRA
     LETLLERGLI EDKGRKEAPG RPILYGTTAE FLRYFGLREL SELPPVEIDT SEPGLIVPTR
     TGGGEAEREV QASLFAGGEE PSAEAADGGA GESTHGEEE