SP0J_THET2
ID SP0J_THET2 Reviewed; 269 AA.
AC Q72H91;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Chromosome-partitioning protein Spo0J;
GN Name=spo0C; Synonyms=parB; OrderedLocusNames=TT_C1604;
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(2004).
RN [2]
RP FUNCTION, AND MUTAGENESIS OF ARG-10.
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15635448; DOI=10.1038/sj.emboj.7600530;
RA Leonard T.A., Butler P.J., Lowe J.;
RT "Bacterial chromosome segregation: structure and DNA binding of the Soj
RT dimer--a conserved biological switch.";
RL EMBO J. 24:270-282(2005).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-222, SUBUNIT, AND DNA-BINDING.
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15228524; DOI=10.1111/j.1365-2958.2004.04133.x;
RA Leonard T.A., Butler P.J., Lowe J.;
RT "Structural analysis of the chromosome segregation protein Spo0J from
RT Thermus thermophilus.";
RL Mol. Microbiol. 53:419-432(2004).
CC -!- FUNCTION: Probably involved in chromosome partitioning. Binds to a
CC plasmid centromere-like site parS. Stimulates the ATPase activity 10-
CC fold of Soj; the first 20 residues may be responsible.
CC {ECO:0000269|PubMed:15635448}.
CC -!- SUBUNIT: Homodimer, probably via the C-terminal 46 residues.
CC Dimerization of the N-terminal H-T-H region may require DNA-binding.
CC Probably interacts with ATPase Soj. {ECO:0000269|PubMed:15228524}.
CC -!- SIMILARITY: Belongs to the ParB family. {ECO:0000305}.
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DR EMBL; AE017221; AAS81946.1; -; Genomic_DNA.
DR RefSeq; WP_011173975.1; NC_005835.1.
DR PDB; 1VZ0; X-ray; 2.30 A; A/B/C/D/E/F/G/H=1-222.
DR PDBsum; 1VZ0; -.
DR AlphaFoldDB; Q72H91; -.
DR SMR; Q72H91; -.
DR STRING; 262724.TT_C1604; -.
DR EnsemblBacteria; AAS81946; AAS81946; TT_C1604.
DR KEGG; tth:TT_C1604; -.
DR eggNOG; COG1475; Bacteria.
DR HOGENOM; CLU_023853_0_0_0; -.
DR OMA; IALSYQR; -.
DR OrthoDB; 653368at2; -.
DR EvolutionaryTrace; Q72H91; -.
DR Proteomes; UP000000592; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR InterPro; IPR041468; HTH_ParB/Spo0J.
DR InterPro; IPR004437; ParB/RepB/Spo0J.
DR InterPro; IPR003115; ParB/Sulfiredoxin_dom.
DR InterPro; IPR036086; ParB/Sulfiredoxin_sf.
DR Pfam; PF17762; HTH_ParB; 1.
DR Pfam; PF02195; ParBc; 1.
DR SMART; SM00470; ParB; 1.
DR SUPFAM; SSF110849; SSF110849; 1.
DR TIGRFAMs; TIGR00180; parB_part; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome partition; DNA-binding.
FT CHAIN 1..269
FT /note="Chromosome-partitioning protein Spo0J"
FT /id="PRO_0000422778"
FT DNA_BIND 137..156
FT /note="H-T-H motif"
FT /evidence="ECO:0000305"
FT REGION 1..20
FT /note="Stimulates ATPase activity of Soj by 8%"
FT REGION 223..269
FT /note="Required for DNA-binding; may be responsible for
FT dimerization"
FT MUTAGEN 10
FT /note="R->A: No longer stimulates ATPase activity of Soj,
FT in the 1-20 peptide."
FT /evidence="ECO:0000269|PubMed:15635448"
FT STRAND 24..27
FT /evidence="ECO:0007829|PDB:1VZ0"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:1VZ0"
FT HELIX 38..57
FT /evidence="ECO:0007829|PDB:1VZ0"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:1VZ0"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:1VZ0"
FT HELIX 78..87
FT /evidence="ECO:0007829|PDB:1VZ0"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:1VZ0"
FT HELIX 101..114
FT /evidence="ECO:0007829|PDB:1VZ0"
FT HELIX 120..132
FT /evidence="ECO:0007829|PDB:1VZ0"
FT HELIX 137..144
FT /evidence="ECO:0007829|PDB:1VZ0"
FT HELIX 148..156
FT /evidence="ECO:0007829|PDB:1VZ0"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:1VZ0"
FT HELIX 162..169
FT /evidence="ECO:0007829|PDB:1VZ0"
FT HELIX 175..182
FT /evidence="ECO:0007829|PDB:1VZ0"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:1VZ0"
FT HELIX 189..198
FT /evidence="ECO:0007829|PDB:1VZ0"
FT HELIX 203..206
FT /evidence="ECO:0007829|PDB:1VZ0"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:1VZ0"
SQ SEQUENCE 269 AA; 29751 MW; 396F2C033BC87671 CRC64;
MSRKPSGLGR GLEALLPKTG AGVVRLPLAS IRPNPRQPRK RFAEESLKEL ADSIREKGLL
QPLLVRPQGD GYELVAGERR YRAALMAGLQ EVPAVVKDLT DREALELALV ENLQREDLSP
VEEARGYQAL LEMGLTQEEV ARRVGKARST VANALRLLQL PPEALEALER GEITAGHARA
LLMLEPEDRL WGLKEILEKG LSVRQAEALR ERLAMAPKRS AEPSPLSLEL SRHLGLPVRV
VGGKKGKVVI QYRSLEELEA LLRRLGYQA
