IED ID | IndEnz0002001957 |
Enzyme Type ID | protease001957 |
Protein Name |
Single-stranded DNA-binding protein, mitochondrial Mt-SSB MtSSB PWP1-interacting protein 17 |
Gene Name | SSBP1 SSBP |
Organism | Homo sapiens (Human) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
Enzyme Sequence | MFRRPVLQVLRQFVRHESETTTSLVLERSLNRVHLLGRVGQDPVLRQVEGKNPVTIFSLATNEMWRSGDSEVYQLGDVSQKTTWHRISVFRPGLRDVAYQYVKKGSRIYLEGKIDYGEYMDKNNVRRQATTIIADNIIFLSDQTKEKE |
Enzyme Length | 148 |
Uniprot Accession Number | Q04837 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | |
Enzyme Function | FUNCTION: Binds preferentially and cooperatively to pyrimidine rich single-stranded DNA (ss-DNA) (PubMed:21953457, PubMed:23290262, PubMed:31550240). In vitro, required to maintain the copy number of mitochondrial DNA (mtDNA) and plays a crucial role during mtDNA replication by stimulating the activity of the replisome components POLG and TWNK at the replication fork (PubMed:21953457, PubMed:12975372, PubMed:26446790, PubMed:15167897, PubMed:31550240). Promotes the activity of the gamma complex polymerase POLG, largely by organizing the template DNA and eliminating secondary structures to favor ss-DNA conformations that facilitate POLG activity (PubMed:26446790, PubMed:21953457, PubMed:31550240). In addition it is able to promote the 5'-3' unwinding activity of the mtDNA helicase TWNK (PubMed:12975372). May also function in mtDNA repair (PubMed:23290262). {ECO:0000269|PubMed:12975372, ECO:0000269|PubMed:15167897, ECO:0000269|PubMed:21953457, ECO:0000269|PubMed:23290262, ECO:0000269|PubMed:26446790, ECO:0000269|PubMed:31550240}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Beta strand (9); Chain (1); Domain (1); Helix (1); Modified residue (4); Mutagenesis (5); Natural variant (7); Transit peptide (1) |
Keywords | 3D-structure;Acetylation;DNA replication;DNA-binding;Direct protein sequencing;Disease variant;Mitochondrion;Mitochondrion nucleoid;Phosphoprotein;Reference proteome;Transit peptide |
Interact With | O75603; P47929; Q7L8S5; Itself; P04618 |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:18063578, ECO:0000269|PubMed:31550237, ECO:0000269|PubMed:31550240}. Mitochondrion matrix, mitochondrion nucleoid {ECO:0000269|PubMed:18063578, ECO:0000269|PubMed:31550240}. |
Modified Residue | MOD_RES 67; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q9CYR0"; MOD_RES 79; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:17525332, ECO:0007744|PubMed:23186163"; MOD_RES 113; /note="N6-acetyllysine"; /evidence="ECO:0007744|PubMed:19608861"; MOD_RES 122; /note="N6-succinyllysine"; /evidence="ECO:0000250|UniProtKB:Q9CYR0" |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | X-ray crystallography (4) |
Cross Reference PDB | 1S3O; 2DUD; 3ULL; 6RUP; |
Mapped Pubmed ID | 12479417; 12577067; 15133161; 18305033; 18457437; 19066201; 19167051; 19738201; 19759019; 19786724; 19805454; 19951946; 20000738; 20186120; 20360068; 20434493; 20562859; 20877624; 21150319; 21242961; 21360678; 21851590; 21911578; 22153281; 22190034; 22575643; 22863774; 23184057; 23871696; 23902751; 23986477; 25036637; 25249620; 25609649; 25762445; 25852190; 26058080; 26170237; 26496610; 26638075; 27938330; 28210897; 28448822; 28486639; 28609781; 28778884; 29182774; 29522991; 29577982; 30256971; 30412255; 30415472; 30715486; 31998294; 33087282; 33671400; 33847964; 33847965; 33847968; 34548540; 34905022; |
Motif | |
Gene Encoded By | |
Mass | 17,260 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |