SOJ_THET2
ID SOJ_THET2 Reviewed; 249 AA.
AC Q72H90;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Chromosome-partitioning ATPase Soj;
DE EC=3.6.-.-;
GN Name=soj; OrderedLocusNames=TT_C1605;
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 X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH ADP OR ATP, FUNCTION
RP AS AN ATPASE, ACTIVITY REGULATION, SUBUNIT, DNA-BINDING, AND MUTAGENESIS OF
RP GLY-16; LYS-20 AND ASP-44.
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).
CC -!- FUNCTION: ATPase probably involved in chromosome partitioning.
CC Cooperatively binds dsDNA, forming nucleoprotein filaments in a
CC strictly ATP-dependent fashion. Can also bind ssDNA with lower
CC affinity. {ECO:0000269|PubMed:15635448}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC -!- ACTIVITY REGULATION: ATPase activity is stimulated 10-fold in the
CC presence of Spo0J and DNA (parS, a plasmid centromere-like site or
CC plasmid DNA itself). The first 20 residues of Spo0J stimulate ATPase by
CC 8%. {ECO:0000269|PubMed:15635448}.
CC -!- SUBUNIT: Monomer in the absence of nucleotides or presence of ADP, in
CC the presence of ATP is found in a monomer-dimer equilibrium. ATP-
CC binding is required for DNA-binding. Probably interacts with Spo0J.
CC {ECO:0000269|PubMed:15635448}.
CC -!- SIMILARITY: Belongs to the ParA family. {ECO:0000305}.
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DR EMBL; AE017221; AAS81947.1; -; Genomic_DNA.
DR RefSeq; WP_011173976.1; NC_005835.1.
DR PDB; 1WCV; X-ray; 1.60 A; 1=1-249.
DR PDB; 2BEJ; X-ray; 2.10 A; A=1-249.
DR PDB; 2BEK; X-ray; 1.80 A; A/B/C/D=1-249.
DR PDBsum; 1WCV; -.
DR PDBsum; 2BEJ; -.
DR PDBsum; 2BEK; -.
DR AlphaFoldDB; Q72H90; -.
DR SMR; Q72H90; -.
DR STRING; 262724.TT_C1605; -.
DR EnsemblBacteria; AAS81947; AAS81947; TT_C1605.
DR KEGG; tth:TT_C1605; -.
DR eggNOG; COG1192; Bacteria.
DR HOGENOM; CLU_037612_1_4_0; -.
DR OMA; VQCEYFA; -.
DR OrthoDB; 729012at2; -.
DR EvolutionaryTrace; Q72H90; -.
DR Proteomes; UP000000592; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR025669; AAA_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF13614; AAA_31; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chromosome partition; DNA-binding; Hydrolase;
KW Nucleotide-binding.
FT CHAIN 1..249
FT /note="Chromosome-partitioning ATPase Soj"
FT /id="PRO_0000422776"
FT BINDING 15..22
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15635448"
FT BINDING 207..212
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MUTAGEN 16
FT /note="G->A: Dimerization-deficient despite ATP-binding."
FT /evidence="ECO:0000269|PubMed:15635448"
FT MUTAGEN 20
FT /note="K->A: Nucleotide-binding-deficient, no ATPase
FT activity, cannot bind DNA. No effect on dimerization."
FT /evidence="ECO:0000269|PubMed:15635448"
FT MUTAGEN 44
FT /note="D->A: ATP hydrolysis-deficient. Forms only dimers in
FT the presence of ATP."
FT /evidence="ECO:0000269|PubMed:15635448"
FT STRAND 8..11
FT /evidence="ECO:0007829|PDB:1WCV"
FT HELIX 18..33
FT /evidence="ECO:0007829|PDB:1WCV"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:1WCV"
FT HELIX 48..52
FT /evidence="ECO:0007829|PDB:1WCV"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:2BEK"
FT HELIX 61..65
FT /evidence="ECO:0007829|PDB:1WCV"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:1WCV"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:1WCV"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:1WCV"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:1WCV"
FT HELIX 90..96
FT /evidence="ECO:0007829|PDB:1WCV"
FT HELIX 102..106
FT /evidence="ECO:0007829|PDB:1WCV"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:1WCV"
FT HELIX 125..133
FT /evidence="ECO:0007829|PDB:1WCV"
FT STRAND 135..144
FT /evidence="ECO:0007829|PDB:1WCV"
FT HELIX 147..164
FT /evidence="ECO:0007829|PDB:1WCV"
FT STRAND 170..179
FT /evidence="ECO:0007829|PDB:1WCV"
FT HELIX 185..197
FT /evidence="ECO:0007829|PDB:1WCV"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:1WCV"
FT HELIX 210..218
FT /evidence="ECO:0007829|PDB:1WCV"
FT HELIX 222..225
FT /evidence="ECO:0007829|PDB:1WCV"
FT HELIX 230..246
FT /evidence="ECO:0007829|PDB:1WCV"
SQ SEQUENCE 249 AA; 26563 MW; 55200FE8AD015DBD CRC64;
MLRAKVRRIA LANQKGGVGK TTTAINLAAY LARLGKRVLL VDLDPQGNAT SGLGVRAERG
VYHLLQGEPL EGLVHPVDGF HLLPATPDLV GATVELAGAP TALREALRDE GYDLVLLDAP
PSLSPLTLNA LAAAEGVVVP VQAEYYALEG VAGLLATLEE VRAGLNPRLR LLGILVTMYD
GRTLLAQQVE AQLRAHFGEK VFWTVIPRNV RLAEAPSFGK TIAQHAPTSP GAHAYRRLAE
EVMARVQEA
