SSBP_RAT
ID SSBP_RAT Reviewed; 151 AA.
AC P28042;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 2.
DT 25-MAY-2022, entry version 150.
DE RecName: Full=Single-stranded DNA-binding protein, mitochondrial;
DE Short=Mt-SSB;
DE Short=MtSSB;
DE AltName: Full=Single strand DNA-binding protein P16;
DE Flags: Precursor;
GN Name=Ssbp1; Synonyms=Ssbp;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=8482537; DOI=10.1016/0378-1119(93)90370-i;
RA Tiranti V., Rocchi M., Didonato S., Zeviani M.;
RT "Cloning of human and rat cDNAs encoding the mitochondrial single-stranded
RT DNA-binding protein (SSB).";
RL Gene 126:219-225(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=9611270; DOI=10.1016/s0378-1119(98)00148-6;
RA Gupta S., van Tuyle G.C.;
RT "The gene and processed pseudogenes of the rat mitochondrial single-strand
RT DNA-binding protein: structure and promoter strength analyses.";
RL Gene 212:269-278(1998).
RN [3]
RP PROTEIN SEQUENCE OF 17-46.
RX PubMed=2221914; DOI=10.1016/0003-9861(90)90094-f;
RA Hoke G.D., Pavco P.A., Ledwith B.J., van Tuyle G.C.;
RT "Structural and functional studies of the rat mitochondrial single strand
RT DNA binding protein P16.";
RL Arch. Biochem. Biophys. 282:116-124(1990).
CC -!- FUNCTION: Binds preferentially and cooperatively to pyrimidine rich
CC single-stranded DNA (ss-DNA). In vitro, required to maintain the copy
CC number of mitochondrial DNA (mtDNA) and plays a crucial role during
CC mtDNA replication by stimulating the activity of the replisome
CC components POLG and TWNK at the replication fork. Promotes the activity
CC of the gamma complex polymerase POLG, largely by organizing the
CC template DNA and eliminating secondary structures to favor ss-DNA
CC conformations that facilitate POLG activity. In addition it is able to
CC promote the 5'-3' unwinding activity of the mtDNA helicase TWNK. May
CC also function in mtDNA repair. {ECO:0000250|UniProtKB:Q04837}.
CC -!- SUBUNIT: Homotetramer. Interacts with MPG/AAG, through inhibition of
CC its glycosylase activity it potentially prevents formation of DNA
CC breaks in ssDNA, ensuring that base removal primarily occurs in dsDNA.
CC Interacts with POLDIP2. Interacts with PRIMPOL.
CC {ECO:0000250|UniProtKB:Q04837}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q04837}.
CC Mitochondrion matrix, mitochondrion nucleoid
CC {ECO:0000250|UniProtKB:Q04837}.
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DR EMBL; M94557; AAA67315.1; -; mRNA.
DR EMBL; AF043635; AAC18063.1; -; Genomic_DNA.
DR EMBL; AF043630; AAC18063.1; JOINED; Genomic_DNA.
DR EMBL; AF043631; AAC18063.1; JOINED; Genomic_DNA.
DR EMBL; AF043632; AAC18063.1; JOINED; Genomic_DNA.
DR EMBL; AF043633; AAC18063.1; JOINED; Genomic_DNA.
DR EMBL; AF043634; AAC18063.1; JOINED; Genomic_DNA.
DR PIR; JN0569; JN0569.
DR AlphaFoldDB; P28042; -.
DR SMR; P28042; -.
DR BioGRID; 248524; 1.
DR IntAct; P28042; 1.
DR STRING; 10116.ENSRNOP00000016217; -.
DR iPTMnet; P28042; -.
DR PhosphoSitePlus; P28042; -.
DR jPOST; P28042; -.
DR PaxDb; P28042; -.
DR PRIDE; P28042; -.
DR UCSC; RGD:3760; rat.
DR RGD; 3760; Ssbp1.
DR eggNOG; KOG1653; Eukaryota.
DR InParanoid; P28042; -.
DR PhylomeDB; P28042; -.
DR PRO; PR:P28042; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0042645; C:mitochondrial nucleoid; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0009295; C:nucleoid; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; ISO:RGD.
DR GO; GO:0006264; P:mitochondrial DNA replication; IBA:GO_Central.
DR GO; GO:0070584; P:mitochondrion morphogenesis; ISO:RGD.
DR GO; GO:1905776; P:positive regulation of DNA helicase activity; ISO:RGD.
DR GO; GO:0051096; P:positive regulation of helicase activity; ISO:RGD.
DR GO; GO:0090297; P:positive regulation of mitochondrial DNA replication; ISS:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR CDD; cd04496; SSB_OBF; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR HAMAP; MF_00984; SSB; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR000424; Primosome_PriB/ssb.
DR InterPro; IPR011344; ssDNA-bd.
DR PANTHER; PTHR10302; PTHR10302; 1.
DR Pfam; PF00436; SSB; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR00621; ssb; 1.
DR PROSITE; PS50935; SSB; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; DNA replication; DNA-binding;
KW Mitochondrion; Mitochondrion nucleoid; Phosphoprotein; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..16
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:2221914"
FT CHAIN 17..151
FT /note="Single-stranded DNA-binding protein, mitochondrial"
FT /id="PRO_0000033265"
FT DOMAIN 30..141
FT /note="SSB"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CYR0"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04837"
FT MOD_RES 113
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q04837"
FT MOD_RES 122
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CYR0"
SQ SEQUENCE 151 AA; 17455 MW; B9CA830AB280D6D9 CRC64;
MFRRPVLQVF RQFVRQESEV ASSLVLERSL NRVQLLGRVG QDPVMRQVEG KNPVTIFSLA
TNEMWRSGDN EAYQMGDVSQ KTTWHRISVF RPGLRDVAYQ YVKKGARIFV EGKVDYGEYM
DKNNVRRQAT TIIADNIIFL SDQAREKPLN G
