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Database: UniProt
Entry: A0A286IK78_9BACT
LinkDB: A0A286IK78_9BACT
Original site: A0A286IK78_9BACT 
ID   A0A286IK78_9BACT        Unreviewed;       149 AA.
AC   A0A286IK78;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Single-stranded DNA-binding protein {ECO:0000256|HAMAP-Rule:MF_00984, ECO:0000256|RuleBase:RU000524};
DE            Short=SSB {ECO:0000256|HAMAP-Rule:MF_00984};
GN   ORFNames=SAMN06298216_1443 {ECO:0000313|EMBL:SOE20969.1};
OS   Spirosomataceae bacterium TFI 002.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae.
OX   NCBI_TaxID=1945892 {ECO:0000313|EMBL:SOE20969.1, ECO:0000313|Proteomes:UP000217493};
RN   [1] {ECO:0000313|EMBL:SOE20969.1, ECO:0000313|Proteomes:UP000217493}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TFI 002 {ECO:0000313|EMBL:SOE20969.1,
RC   ECO:0000313|Proteomes:UP000217493};
RA   Ehlers B., Leendertz F.H.;
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays an important role in DNA replication, recombination and
CC       repair. Binds to ssDNA and to an array of partner proteins to recruit
CC       them to their sites of action during DNA metabolism.
CC       {ECO:0000256|HAMAP-Rule:MF_00984}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00984}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00984}.
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DR   EMBL; LT907983; SOE20969.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A286IK78; -.
DR   OrthoDB; 9809878at2; -.
DR   Proteomes; UP000217493; Chromosome i.
DR   GO; GO:0003697; F:single-stranded DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR   CDD; cd04496; SSB_OBF; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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   NCBIfam; TIGR00621; ssb; 1.
DR   PANTHER; PTHR10302; SINGLE-STRANDED DNA-BINDING PROTEIN; 1.
DR   PANTHER; PTHR10302:SF0; SINGLE-STRANDED DNA-BINDING PROTEIN, MITOCHONDRIAL; 1.
DR   Pfam; PF00436; SSB; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS50935; SSB; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_00984};
KW   DNA recombination {ECO:0000256|HAMAP-Rule:MF_00984};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_00984};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00984};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00984}; Reference proteome {ECO:0000313|Proteomes:UP000217493}.
FT   REGION          84..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           144..149
FT                   /note="Important for interaction with partner proteins"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00984"
FT   COMPBIAS        109..139
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   149 AA;  16300 MW;  72F28F888BBEDF1E CRC64;
     MAGLNKVLLI GNVGGDPEIR SLPSGSKVAN FSLATSESYN DKSGQKQTVT EWHRIELWDG
     LATIAERYVK KGDPIYIEGK IRNERWTDKD GQEKTGVRIR GLSMQMLGSA RGGDNNYGNQ
     EDDSQSSGHT LSEPDNSLVN NGGEDDLPF
//
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