ID   SCPB_STAAW              Reviewed;         180 AA.
AC   Q8NWF2;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Segregation and condensation protein B {ECO:0000255|HAMAP-Rule:MF_01804};
GN   Name=scpB {ECO:0000255|HAMAP-Rule:MF_01804}; OrderedLocusNames=MW1448;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA   Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-acquired
RT   MRSA.";
RL   Lancet 359:1819-1827(2002).
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; BA000033; BAB95313.1; -; Genomic_DNA.
DR   RefSeq; WP_000368657.1; NC_003923.1.
DR   AlphaFoldDB; Q8NWF2; -.
DR   SMR; Q8NWF2; -.
DR   EnsemblBacteria; BAB95313; BAB95313; BAB95313.
DR   KEGG; sam:MW1448; -.
DR   HOGENOM; CLU_045647_5_3_9; -.
DR   OMA; DGWRFYT; -.
DR   Proteomes; UP000000418; 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   3: Inferred from homology;
KW   Cell cycle; Cell division; Chromosome partition; Cytoplasm.
FT   CHAIN           1..180
FT                   /note="Segregation and condensation protein B"
FT                   /id="PRO_0000211150"
SQ   SEQUENCE   180 AA;  20205 MW;  D9DF3E2F33E44E88 CRC64;
     MDNHGILESL LFTAGDEGLD EKQLLEILDM SKNQLVELIE NYSSHGLMIQ RFGTTYVLTT
     KKEAATYIEQ LIEQKSQMKL SQAAMEVLSI IAYNQPLSRS DIELIRSINS DGAVKTLIAK
     GLVEAKVVNE QRSQQLITTD LFLNVFGISN IEDLPTTEED DEEMDAFFSN LVNQKGENND