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Database: UniProt
Entry: A0A1H3RGN7_9FIRM
LinkDB: A0A1H3RGN7_9FIRM
Original site: A0A1H3RGN7_9FIRM 
ID   A0A1H3RGN7_9FIRM        Unreviewed;       152 AA.
AC   A0A1H3RGN7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Single-stranded DNA-binding protein {ECO:0000256|HAMAP-Rule:MF_00984, ECO:0000256|PIRNR:PIRNR002070};
DE            Short=SSB {ECO:0000256|HAMAP-Rule:MF_00984};
GN   ORFNames=SAMN05660462_02374 {ECO:0000313|EMBL:SDZ24826.1};
OS   Proteiniborus ethanoligenes.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Proteiniborus.
OX   NCBI_TaxID=415015 {ECO:0000313|EMBL:SDZ24826.1, ECO:0000313|Proteomes:UP000198625};
RN   [1] {ECO:0000313|EMBL:SDZ24826.1, ECO:0000313|Proteomes:UP000198625}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21650 {ECO:0000313|EMBL:SDZ24826.1,
RC   ECO:0000313|Proteomes:UP000198625};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FNQE01000027; SDZ24826.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H3RGN7; -.
DR   STRING; 415015.SAMN05660462_02374; -.
DR   OrthoDB; 9809878at2; -.
DR   Proteomes; UP000198625; Unassembled WGS sequence.
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:SF27; SINGLE-STRANDED DNA-BINDING PROTEIN; 1.
DR   Pfam; PF00436; SSB; 1.
DR   PIRSF; PIRSF002070; 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:UP000198625}.
FT   MOTIF           147..152
FT                   /note="Important for interaction with partner proteins"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00984"
SQ   SEQUENCE   152 AA;  17080 MW;  BE1496AAE309C854 CRC64;
     MNSVILIGRL TRDPELRYLS SGMAVSRFSI AVDKNHLSRE KKQELESKGQ PTADFINIVV
     WGKQAENCAN YLVKGRLVGI QGRIQTGSYT AQDGTKRYTT DVVADRVQFL EWGDSKQGSQ
     NTNRDFNSMN RDFDAGIDMD GFHPADDDDI PF
//
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