ID   SCPB_BACSU              Reviewed;         197 AA.
AC   P35155;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Segregation and condensation protein B;
GN   Name=scpB; Synonyms=ypuH; OrderedLocusNames=BSU23210;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC   3610 / NRRL NRS-744 / VKM B-501;
RX   PubMed=7934829; DOI=10.1111/j.1365-2958.1993.tb02670.x;
RA   Sorokin A.V., Zumstein E., Azevedo V., Ehrlich S.D., Serror P.;
RT   "The organization of the Bacillus subtilis 168 chromosome region between
RT   the spoVA and serA genetic loci, based on sequence data.";
RL   Mol. Microbiol. 10:385-395(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   INTERACTION WITH SCPA AND SMC.
RX   PubMed=12065423; DOI=10.1093/emboj/cdf314;
RA   Mascarenhas J., Soppa J., Strunnikov A.V., Graumann P.L.;
RT   "Cell cycle-dependent localization of two novel prokaryotic chromosome
RT   segregation and condensation proteins in Bacillus subtilis that interact
RT   with SMC protein.";
RL   EMBO J. 21:3108-3118(2002).
RN   [4]
RP   CHARACTERIZATION.
RX   PubMed=12100548; DOI=10.1046/j.1365-2958.2002.03012.x;
RA   Soppa J., Kobayashi K., Noirot-Gros M.-F., Oesterhelt D., Ehrlich S.D.,
RA   Dervyn E., Ogasawara N., Moriya S.;
RT   "Discovery of two novel families of proteins that are proposed to interact
RT   with prokaryotic SMC proteins, and characterization of the Bacillus
RT   subtilis family members ScpA and ScpB.";
RL   Mol. Microbiol. 45:59-71(2002).
RN   [5]
RP   SUBCELLULAR LOCATION, HOMODIMERIZATION, AND INTERACTION WITH SMC AND SCPA.
RX   PubMed=12897137; DOI=10.1128/mcb.23.16.5638-5650.2003;
RA   Volkov A., Mascarenhas J., Andrei-Selmer C., Ulrich H.D., Graumann P.L.;
RT   "A prokaryotic condensin/cohesin-like complex can actively compact
RT   chromosomes from a single position on the nucleoid and binds to DNA as a
RT   ring-like structure.";
RL   Mol. Cell. Biol. 23:5638-5650(2003).
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   -!- 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   -!- INTERACTION:
CC       P35155; P35154: scpA; NbExp=5; IntAct=EBI-2121445, EBI-2121359;
CC       P35155; P51834: smc; NbExp=2; IntAct=EBI-2121445, EBI-2121372;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12897137}.
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.
CC   -!- SIMILARITY: Belongs to the ScpB family. {ECO:0000305}.
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DR   EMBL; L09228; AAA67488.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14253.1; -; Genomic_DNA.
DR   PIR; S45550; S45550.
DR   RefSeq; NP_390202.1; NC_000964.3.
DR   RefSeq; WP_003223904.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; P35155; -.
DR   SMR; P35155; -.
DR   DIP; DIP-52409N; -.
DR   IntAct; P35155; 2.
DR   STRING; 224308.BSU23210; -.
DR   PaxDb; P35155; -.
DR   PRIDE; P35155; -.
DR   EnsemblBacteria; CAB14253; CAB14253; BSU_23210.
DR   GeneID; 64304102; -.
DR   GeneID; 938951; -.
DR   KEGG; bsu:BSU23210; -.
DR   PATRIC; fig|224308.179.peg.2528; -.
DR   eggNOG; COG1386; Bacteria.
DR   InParanoid; P35155; -.
DR   OMA; DGWRFYT; -.
DR   PhylomeDB; P35155; -.
DR   BioCyc; BSUB:BSU23210-MON; -.
DR   PRO; PR:P35155; -.
DR   Proteomes; UP000001570; 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..197
FT                   /note="Segregation and condensation protein B"
FT                   /id="PRO_0000211127"
SQ   SEQUENCE   197 AA;  22038 MW;  77D27E0040A9D6F1 CRC64;
     MGLDIVNWKA IVEALLYAAG DEGLTKKQLL TVLEIEEPEL NTIMADVADE YRGDTRGIEL
     IEYADTYMLS TKKDFAPYLK KLIEVPSKGL SQASLEVLAI VSYKQPITRA EIEEIRGVKS
     ERILHSLVAK ALLCEVGRAD GPGRAILYGT TPTFLEQFGL KTLDELPPLP ENAEEDVLQE
     EADLFFENFN QTFEDIK