SCPB_LACLM
ID SCPB_LACLM Reviewed; 188 AA.
AC A2RKH6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-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=llmg_1193;
OS Lactococcus lactis subsp. cremoris (strain MG1363).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus; Lactococcus cremoris subsp. cremoris.
OX NCBI_TaxID=416870;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MG1363;
RX PubMed=17307855; DOI=10.1128/jb.01768-06;
RA Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA van Sinderen D., Kok J.;
RT "The complete genome sequence of the lactic acid bacterial paradigm
RT Lactococcus lactis subsp. cremoris MG1363.";
RL J. Bacteriol. 189:3256-3270(2007).
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; AM406671; CAL97786.1; -; Genomic_DNA.
DR RefSeq; WP_011676203.1; NC_009004.1.
DR AlphaFoldDB; A2RKH6; -.
DR SMR; A2RKH6; -.
DR STRING; 416870.llmg_1193; -.
DR PRIDE; A2RKH6; -.
DR EnsemblBacteria; CAL97786; CAL97786; llmg_1193.
DR GeneID; 61109531; -.
DR KEGG; llm:llmg_1193; -.
DR eggNOG; COG1386; Bacteria.
DR HOGENOM; CLU_045647_5_3_9; -.
DR OMA; DGWRFYT; -.
DR PhylomeDB; A2RKH6; -.
DR BioCyc; LLAC416870:LLMG_RS06040-MON; -.
DR Proteomes; UP000000364; 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..188
FT /note="Segregation and condensation protein B"
FT /id="PRO_1000069956"
SQ SEQUENCE 188 AA; 21174 MW; 383C9A544311CBD6 CRC64;
MNKTATCELL LFVSGEAGLT LTELSSLTEM SKQACQQQID YLKEKYHSDR ESALTIIETA
GKYRMATKED FSEILKNYAK TPLNQSLSKS ALEVLSIIAY KQPLTRIEID QLRGVNSSGV
LSTLRAFDLV EKVGQVEAPG RPSLYATTEF FLDYIGINNL EELPEIDESR YVAEQQTLFN
ESEENENQ