SCPB_STRR6
ID SCPB_STRR6 Reviewed; 189 AA.
AC Q8DNI9; Q9EUQ6;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Segregation and condensation protein B {ECO:0000255|HAMAP-Rule:MF_01804};
GN Name=scpB {ECO:0000255|HAMAP-Rule:MF_01804}; OrderedLocusNames=spr1690;
OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=171101;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11763967;
RA Reichmann P., Hakenbeck R.;
RT "A XerD recombinase with unusual active site motifs in Streptococcus
RT pneumoniae.";
RL J. Mol. Microbiol. Biotechnol. 4:101-110(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL J. Bacteriol. 183:5709-5717(2001).
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 -!- INTERACTION:
CC Q8DNI9; Q9EUQ7: scpA; NbExp=4; IntAct=EBI-16033389, EBI-16033375;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC19450.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ277766; CAC19450.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AE007317; AAL00493.1; -; Genomic_DNA.
DR PIR; H98082; H98082.
DR RefSeq; NP_359282.1; NC_003098.1.
DR RefSeq; WP_000105310.1; NC_003098.1.
DR AlphaFoldDB; Q8DNI9; -.
DR SMR; Q8DNI9; -.
DR DIP; DIP-60234N; -.
DR IntAct; Q8DNI9; 1.
DR STRING; 171101.spr1690; -.
DR EnsemblBacteria; AAL00493; AAL00493; spr1690.
DR GeneID; 60232689; -.
DR GeneID; 66806948; -.
DR KEGG; spr:spr1690; -.
DR PATRIC; fig|171101.6.peg.1828; -.
DR eggNOG; COG1386; Bacteria.
DR HOGENOM; CLU_045647_5_3_9; -.
DR OMA; DGWRFYT; -.
DR Proteomes; UP000000586; 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 1: Evidence at protein level;
KW Cell cycle; Cell division; Chromosome partition; Cytoplasm;
KW Reference proteome.
FT CHAIN 1..189
FT /note="Segregation and condensation protein B"
FT /id="PRO_0000211160"
SQ SEQUENCE 189 AA; 21038 MW; B69B8B46CAED599A CRC64;
MSTLAKIEAL LFVAGEDGIR VRQLAELLSL PPTGIQQSLG KLAQKYEKDP DSSLALIETS
GAYRLVTKPQ FAEILKEYSK APINQSLSRA ALETLSIIAY KQPITRIEID AIRGVNSSGA
LAKLQAFDLI KEDGKKEVLG RPNLYVTTDY FLDYMGINHL EELPVIDELE IQAQESQLFG
ERIEEDENQ