ID   SCPB_STRZP              Reviewed;         189 AA.
AC   C1CMI5;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Segregation and condensation protein B {ECO:0000255|HAMAP-Rule:MF_01804};
GN   Name=scpB {ECO:0000255|HAMAP-Rule:MF_01804}; OrderedLocusNames=SPP_1875;
OS   Streptococcus pneumoniae (strain P1031).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=488223;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P1031;
RX   PubMed=21034474; DOI=10.1186/gb-2010-11-10-r107;
RA   Donati C., Hiller N.L., Tettelin H., Muzzi A., Croucher N.J.,
RA   Angiuoli S.V., Oggioni M., Dunning Hotopp J.C., Hu F.Z., Riley D.R.,
RA   Covacci A., Mitchell T.J., Bentley S.D., Kilian M., Ehrlich G.D.,
RA   Rappuoli R., Moxon E.R., Masignani V.;
RT   "Structure and dynamics of the pan-genome of Streptococcus pneumoniae and
RT   closely related species.";
RL   Genome Biol. 11:R107.1-R107.19(2010).
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; CP000920; ACO20208.1; -; Genomic_DNA.
DR   RefSeq; WP_000105310.1; NC_012467.1.
DR   PDB; 4I98; X-ray; 2.80 A; B/C=1-183.
DR   PDBsum; 4I98; -.
DR   AlphaFoldDB; C1CMI5; -.
DR   SMR; C1CMI5; -.
DR   GeneID; 60232689; -.
DR   GeneID; 66806948; -.
DR   KEGG; spp:SPP_1875; -.
DR   HOGENOM; CLU_045647_5_3_9; -.
DR   OMA; DGWRFYT; -.
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   3D-structure; Cell cycle; Cell division; Chromosome partition; Cytoplasm.
FT   CHAIN           1..189
FT                   /note="Segregation and condensation protein B"
FT                   /id="PRO_1000187546"
FT   HELIX           3..13
FT                   /evidence="ECO:0007829|PDB:4I98"
FT   TURN            14..17
FT                   /evidence="ECO:0007829|PDB:4I98"
FT   HELIX           21..28
FT                   /evidence="ECO:0007829|PDB:4I98"
FT   HELIX           32..48
FT                   /evidence="ECO:0007829|PDB:4I98"
FT   STRAND          54..59
FT                   /evidence="ECO:0007829|PDB:4I98"
FT   STRAND          62..67
FT                   /evidence="ECO:0007829|PDB:4I98"
FT   HELIX           69..71
FT                   /evidence="ECO:0007829|PDB:4I98"
FT   HELIX           72..78
FT                   /evidence="ECO:0007829|PDB:4I98"
FT   HELIX           83..85
FT                   /evidence="ECO:0007829|PDB:4I98"
FT   HELIX           89..101
FT                   /evidence="ECO:0007829|PDB:4I98"
FT   STRAND          103..105
FT                   /evidence="ECO:0007829|PDB:4I98"
FT   HELIX           106..113
FT                   /evidence="ECO:0007829|PDB:4I98"
FT   HELIX           118..126
FT                   /evidence="ECO:0007829|PDB:4I98"
FT   STRAND          129..135
FT                   /evidence="ECO:0007829|PDB:4I98"
FT   STRAND          143..147
FT                   /evidence="ECO:0007829|PDB:4I98"
FT   HELIX           149..155
FT                   /evidence="ECO:0007829|PDB:4I98"
FT   HELIX           160..162
FT                   /evidence="ECO:0007829|PDB:4I98"
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