ID   SSBP_BOVIN              Reviewed;         148 AA.
AC   Q32PB0;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Single-stranded DNA-binding protein, mitochondrial;
DE            Short=Mt-SSB;
DE            Short=MtSSB;
DE   Flags: Precursor;
GN   Name=SSBP1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
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; BC108189; AAI08190.1; -; mRNA.
DR   RefSeq; NP_001032543.1; NM_001037466.1.
DR   AlphaFoldDB; Q32PB0; -.
DR   SMR; Q32PB0; -.
DR   STRING; 9913.ENSBTAP00000014520; -.
DR   PaxDb; Q32PB0; -.
DR   PeptideAtlas; Q32PB0; -.
DR   PRIDE; Q32PB0; -.
DR   GeneID; 515765; -.
DR   KEGG; bta:515765; -.
DR   CTD; 6742; -.
DR   eggNOG; KOG1653; Eukaryota.
DR   InParanoid; Q32PB0; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0042645; C:mitochondrial nucleoid; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0031090; C:organelle membrane; IEA:UniProt.
DR   GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR   GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
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   PIRSF; PIRSF002070; SSB; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00621; ssb; 1.
DR   PROSITE; PS50935; SSB; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; DNA replication; DNA-binding; Mitochondrion;
KW   Mitochondrion nucleoid; Phosphoprotein; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..16
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250|UniProtKB:Q04837"
FT   CHAIN           17..148
FT                   /note="Single-stranded DNA-binding protein, mitochondrial"
FT                   /id="PRO_0000365067"
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   148 AA;  17208 MW;  0CE02136D82696A0 CRC64;
     MFRRPVVQVL RQFVRHESEV ASSLVLERSL NRVQLLGRVG QDPVMRQVEG KNPDTIFSLA
     TNEMWRSGEN ETYQMGDVSQ KTTWHRISVF RPGLRDVAYQ YVKKGSRIYV EGKVDYGEYT
     DKNNVRRQAT TIIADNIIFL SDQIKEKP