ID   SCPA_LACLM              Reviewed;         242 AA.
AC   A2RKH5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Segregation and condensation protein A {ECO:0000255|HAMAP-Rule:MF_01805};
GN   Name=scpA {ECO:0000255|HAMAP-Rule:MF_01805}; OrderedLocusNames=llmg_1192;
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 ScpB that pull DNA away from mid-cell into both cell halves.
CC       {ECO:0000255|HAMAP-Rule:MF_01805}.
CC   -!- SUBUNIT: Component of a cohesin-like complex composed of ScpA, ScpB and
CC       the Smc homodimer, in which ScpA and ScpB bind to the head domain of
CC       Smc. The presence of the three proteins is required for the association
CC       of the complex with DNA. {ECO:0000255|HAMAP-Rule:MF_01805}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01805}.
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_01805}.
CC   -!- SIMILARITY: Belongs to the ScpA family. {ECO:0000255|HAMAP-
CC       Rule:MF_01805}.
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DR   EMBL; AM406671; CAL97785.1; -; Genomic_DNA.
DR   RefSeq; WP_011835091.1; NZ_WJVF01000010.1.
DR   AlphaFoldDB; A2RKH5; -.
DR   SMR; A2RKH5; -.
DR   STRING; 416870.llmg_1192; -.
DR   EnsemblBacteria; CAL97785; CAL97785; llmg_1192.
DR   KEGG; llm:llmg_1192; -.
DR   eggNOG; COG1354; Bacteria.
DR   HOGENOM; CLU_038686_3_3_9; -.
DR   OMA; YLVMAAM; -.
DR   PhylomeDB; A2RKH5; -.
DR   BioCyc; LLAC416870:LLMG_RS06035-MON; -.
DR   Proteomes; UP000000364; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-UniRule.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.10.580; -; 1.
DR   HAMAP; MF_01805; ScpA; 1.
DR   InterPro; IPR003768; ScpA.
DR   InterPro; IPR023093; ScpA-like_C.
DR   PANTHER; PTHR33969; PTHR33969; 1.
DR   Pfam; PF02616; SMC_ScpA; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Chromosome partition; Cytoplasm.
FT   CHAIN           1..242
FT                   /note="Segregation and condensation protein A"
FT                   /id="PRO_1000069972"
SQ   SEQUENCE   242 AA;  28563 MW;  4AB2E019D19BD2B1 CRC64;
     MIKEINIKIK NFEGPLDLLL HLVSQYEMDI FEVPLVPVIE QYLIYIQTMK ELELELAGEY
     MLMASQLMLI KSRRLLPTVT ETFIEDTEQL EYDLLAQIDE YRKYKMLSED LDELHQERSH
     YYSKSKTEII TDETVLLQDK TALDLFLAFS KILELQRQQI EDDNTMIAAE KFTIADKIFE
     LNQKFTEQKI CKFTDLFSDK TNKDELVTTF MALLELIKNQ QVSFSQGELF GEIILERKEI
     SE