ID   SCPB_MYCPU              Reviewed;         207 AA.
AC   Q98R94;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Segregation and condensation protein B {ECO:0000255|HAMAP-Rule:MF_01804};
GN   Name=scpB {ECO:0000255|HAMAP-Rule:MF_01804}; OrderedLocusNames=MYPU_1160;
OS   Mycoplasmopsis pulmonis (strain UAB CTIP) (Mycoplasma pulmonis).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX   NCBI_TaxID=272635;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAB CTIP;
RX   PubMed=11353084; DOI=10.1093/nar/29.10.2145;
RA   Chambaud I., Heilig R., Ferris S., Barbe V., Samson D., Galisson F.,
RA   Moszer I., Dybvig K., Wroblewski H., Viari A., Rocha E.P.C., Blanchard A.;
RT   "The complete genome sequence of the murine respiratory pathogen Mycoplasma
RT   pulmonis.";
RL   Nucleic Acids Res. 29:2145-2153(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   -!- 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; AL445563; CAC13289.1; -; Genomic_DNA.
DR   PIR; D90526; D90526.
DR   AlphaFoldDB; Q98R94; -.
DR   SMR; Q98R94; -.
DR   STRING; 272635.MYPU_1160; -.
DR   EnsemblBacteria; CAC13289; CAC13289; CAC13289.
DR   KEGG; mpu:MYPU_1160; -.
DR   eggNOG; COG1386; Bacteria.
DR   HOGENOM; CLU_045647_5_3_14; -.
DR   OMA; DGWRFYT; -.
DR   Proteomes; UP000000528; 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; 1.
DR   TIGRFAMs; TIGR00281; TIGR00281; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Chromosome partition; Cytoplasm;
KW   Reference proteome.
FT   CHAIN           1..207
FT                   /note="Segregation and condensation protein B"
FT                   /id="PRO_0000211143"
SQ   SEQUENCE   207 AA;  23761 MW;  CAACA84EF8EC460D CRC64;
     MVQLELKKDQ IMKNKIIEAL MYFQGDQGLS PEQVKEVFDL EKDQEGKKLL NDFMEFYNAR
     EGGTKVFVFG EIYKIATIEP LKDYVSKLVS IVRYQKLSKA AIEVAGIVAY KQPITKSMIN
     EIRGVASDQV VNTLLVKNLI EEVGISPTPG KPVLYGITNK FYDYFKIKSL QELPNLSEFD
     FVQSIDEEQE EEQSYEGFNL FSSQREN