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SSBPB_XENLA
ID   SSBPB_XENLA             Reviewed;         148 AA.
AC   P09381; A2RVB2; O13264;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 4.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Single-stranded DNA-binding protein 1-B, mitochondrial;
DE   AltName: Full=Single-stranded DNA-binding protein 2, mitochondrial;
DE            Short=MtSSB-2;
DE            Short=XlSSB2;
DE   AltName: Full=Single-stranded DNA-binding protein R, mitochondrial;
DE            Short=MtSSBr;
DE   Flags: Precursor;
GN   Name=ssbp1-b; Synonyms=mtssb2;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9016954; DOI=10.1016/s0378-1119(96)00574-4;
RA   Champagne A.M., Dufresne C., Viney L., Gueride M.;
RT   "Cloning, sequencing and expression of the two genes encoding the
RT   mitochondrial single-stranded DNA-binding protein in Xenopus laevis.";
RL   Gene 184:65-71(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 18-99.
RX   PubMed=1952953; DOI=10.1016/0003-9861(91)90152-9;
RA   Ghrir R., Lecaer J.-P., Dufresne C., Barat-Gueride M.;
RT   "Primary structure of the two variants of Xenopus laevis mtSSB, a
RT   mitochondrial DNA binding protein.";
RL   Arch. Biochem. Biophys. 291:395-400(1991).
RN   [4]
RP   PRELIMINARY PROTEIN SEQUENCE OF 18-38.
RX   PubMed=3042458; DOI=10.1016/0014-5793(88)81276-6;
RA   Mahoungou C., Ghrir R., Lecaer J.-P., Mignotte B., Barat-Gueride M.;
RT   "The amino-terminal sequence of the Xenopus laevis mitochondrial SSB is
RT   homologous to that of the Escherichia coli protein.";
RL   FEBS Lett. 235:267-270(1988).
CC   -!- FUNCTION: Binds preferentially and cooperatively to pyrimidine rich
CC       single-stranded DNA (ss-DNA). Required to maintain the copy number of
CC       mitochondrial DNA (mtDNA) and plays crucial roles during mtDNA
CC       replication that stimulate activity of the DNA polymerase at the
CC       replication fork. May also function in mtDNA repair.
CC       {ECO:0000250|UniProtKB:Q04837}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q04837}.
CC       Mitochondrion matrix, mitochondrion nucleoid
CC       {ECO:0000250|UniProtKB:Q04837}.
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DR   EMBL; X83674; CAA58648.1; -; Genomic_DNA.
DR   EMBL; BC133265; AAI33266.1; -; mRNA.
DR   PIR; JC6172; JC6172.
DR   RefSeq; NP_001091326.1; NM_001097857.1.
DR   AlphaFoldDB; P09381; -.
DR   SMR; P09381; -.
DR   DNASU; 100037159; -.
DR   GeneID; 100037159; -.
DR   KEGG; xla:100037159; -.
DR   CTD; 100037159; -.
DR   Xenbase; XB-GENE-979715; ssbp1.S.
DR   Proteomes; UP000186698; Chromosome 3S.
DR   Bgee; 100037159; Expressed in oocyte and 19 other tissues.
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   1: Evidence at protein level;
KW   Direct protein sequencing; DNA replication; DNA-binding; Mitochondrion;
KW   Mitochondrion nucleoid; Reference proteome; Transit peptide.
FT   TRANSIT         1..17
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:1952953"
FT   CHAIN           18..148
FT                   /note="Single-stranded DNA-binding protein 1-B,
FT                   mitochondrial"
FT                   /id="PRO_0000033267"
FT   DOMAIN          30..142
FT                   /note="SSB"
FT   CONFLICT        49
FT                   /note="D -> E (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        142
FT                   /note="T -> S (in Ref. 1; CAA58648)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   148 AA;  16943 MW;  6DDA54C91779EC13 CRC64;
     MFHRPVLQVF RQFARCQSTD SLSAILERSM NKVQLLGRVG QDPVMRQADG KNPVTIFSLA
     TNELWRSGEN EVFQPAGDVN QKTTWHRVSV FRPGLRDVAY QHVKKGARLL VEGKIDYGEY
     TDKNNVRRQA TTIIADNIIF LTDLRDKP
 
 
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