SCPB_SYNC1
ID SCPB_SYNC1 Reviewed; 197 AA.
AC Q3A508;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2013, sequence version 2.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Segregation and condensation protein B {ECO:0000255|HAMAP-Rule:MF_01804};
GN Name=scpB {ECO:0000255|HAMAP-Rule:MF_01804}; OrderedLocusNames=Pcar_1300;
OS Syntrophotalea carbinolica (strain DSM 2380 / NBRC 103641 / GraBd1)
OS (Pelobacter carbinolicus).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Syntrophotaleaceae; Syntrophotalea.
OX NCBI_TaxID=338963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2380 / NBRC 103641 / GraBd1;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chertkov O., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Pelobacter carbinolicus DSM 2380.";
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000142; ABA88549.2; -; Genomic_DNA.
DR RefSeq; WP_011341024.1; NC_007498.2.
DR AlphaFoldDB; Q3A508; -.
DR SMR; Q3A508; -.
DR STRING; 338963.Pcar_1300; -.
DR EnsemblBacteria; ABA88549; ABA88549; Pcar_1300.
DR KEGG; pca:Pcar_1300; -.
DR eggNOG; COG1386; Bacteria.
DR HOGENOM; CLU_045647_5_3_7; -.
DR OrthoDB; 1771906at2; -.
DR Proteomes; UP000002534; 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 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;
KW Reference proteome.
FT CHAIN 1..197
FT /note="Segregation and condensation protein B"
FT /id="PRO_0000273305"
SQ SEQUENCE 197 AA; 21621 MW; CA076BE3C438A7C3 CRC64;
MDTVELKAII EALLFAAPGP VRLEQLALAA DADPARVAPL LAELETEYLR AGRGFVLVEL
AEGYQLRTRP EHAEWVRRLH SSRPTRLSRA ALEALAIIAY QQPVTRADID YLRGVDSGGV
VKSLLDKRLV RIVGKKDVPG RPLLYGTSRE FLEFFGLRSL SDLPTLKEFT ELTKESESLL
FDFDAGAGGA TASSEQA