ID   SSBP_RABIT              Reviewed;         148 AA.
AC   Q95KK4;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Single-stranded DNA-binding protein, mitochondrial;
DE            Short=Mt-SSB;
DE            Short=MtSSB;
DE   Flags: Precursor;
GN   Name=SSBP1; Synonyms=SSB;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Dufresne C., Gueride M.;
RT   "Identification and expression of cDNA and pseudogene coding for the rabbit
RT   mitochondrial single-strand DNA-binding protein.";
RL   Submitted (MAY-2001) 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; AJ311162; CAC38115.1; -; mRNA.
DR   RefSeq; NP_001075600.1; NM_001082131.1.
DR   AlphaFoldDB; Q95KK4; -.
DR   SMR; Q95KK4; -.
DR   STRING; 9986.ENSOCUP00000021419; -.
DR   GeneID; 100008866; -.
DR   KEGG; ocu:100008866; -.
DR   CTD; 6742; -.
DR   eggNOG; KOG1653; Eukaryota.
DR   InParanoid; Q95KK4; -.
DR   OrthoDB; 1304218at2759; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0042645; C:mitochondrial nucleoid; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
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_5000067449"
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;  17156 MW;  9AF894B6468C6C43 CRC64;
     MFRRPALQVL RQFVRHESEI ASSLVLERSL NRVQLLGRVG QDPVMRQVEG KNPVTIFSLA
     TNEMWRSGDN ETYQMGDVSQ KTTWHRISVF RPGLRDVAYQ YVKKGSRIYV EGKVDYGEYM
     DKNNVRRQAT TIIADNIVFL SDQTKEKA