SCPB_MOOTA
ID SCPB_MOOTA Reviewed; 195 AA.
AC Q2RIR6;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Segregation and condensation protein B {ECO:0000255|HAMAP-Rule:MF_01804};
GN Name=scpB {ECO:0000255|HAMAP-Rule:MF_01804}; OrderedLocusNames=Moth_1360;
OS Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Moorella group; Moorella.
OX NCBI_TaxID=264732;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39073 / JCM 9320;
RX PubMed=18631365; DOI=10.1111/j.1462-2920.2008.01679.x;
RA Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C.,
RA Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.;
RT "The complete genome sequence of Moorella thermoacetica (f. Clostridium
RT thermoaceticum).";
RL Environ. Microbiol. 10:2550-2573(2008).
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; CP000232; ABC19673.1; -; Genomic_DNA.
DR RefSeq; WP_011392873.1; NC_007644.1.
DR RefSeq; YP_430216.1; NC_007644.1.
DR AlphaFoldDB; Q2RIR6; -.
DR SMR; Q2RIR6; -.
DR STRING; 264732.Moth_1360; -.
DR EnsemblBacteria; ABC19673; ABC19673; Moth_1360.
DR KEGG; mta:Moth_1360; -.
DR PATRIC; fig|264732.11.peg.1459; -.
DR eggNOG; COG1386; Bacteria.
DR HOGENOM; CLU_045647_5_2_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 3: Inferred from homology;
KW Cell cycle; Cell division; Chromosome partition; Cytoplasm.
FT CHAIN 1..195
FT /note="Segregation and condensation protein B"
FT /id="PRO_0000273304"
FT REGION 169..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 195 AA; 21161 MW; 172F6B3682D08D60 CRC64;
MPLFFSDNLR AALECLLFVA GGPVSVDSLA ACLGVKPGDV DELAAELQEL YAREERGLQI
RAVAGGYQMC TRPEFASYCE ALLRPELPAL SRAALETLAI IAYRQPVTRT EMEYIRGVKV
DGVLNTLISR GLVQEVGRKE APGRPILYGT TPKFLEFFGL KDLKELPPLE DVAASQENSR
EAGGRGSIPG HPGEE