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Database: UniProt
Entry: A0A1I1BRY1_9BACL
LinkDB: A0A1I1BRY1_9BACL
Original site: A0A1I1BRY1_9BACL 
ID   A0A1I1BRY1_9BACL        Unreviewed;       180 AA.
AC   A0A1I1BRY1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
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=SAMN05216312_111261 {ECO:0000313|EMBL:SFB52917.1};
OS   Cohnella sp. OV330.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Cohnella.
OX   NCBI_TaxID=1855288 {ECO:0000313|EMBL:SFB52917.1, ECO:0000313|Proteomes:UP000198686};
RN   [1] {ECO:0000313|EMBL:SFB52917.1, ECO:0000313|Proteomes:UP000198686}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OV330 {ECO:0000313|EMBL:SFB52917.1,
RC   ECO:0000313|Proteomes:UP000198686};
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; FOKE01000011; SFB52917.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I1BRY1; -.
DR   Proteomes; UP000198686; 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   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:UP000198686}.
FT   REGION          107..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           175..180
FT                   /note="Important for interaction with partner proteins"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00984"
FT   COMPBIAS        144..161
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   180 AA;  19137 MW;  C0F17299E4590033 CRC64;
     MLNRVILIGR LTKDPELRYT PAGVAVAQFT LAVDRPFSRD SGGGEREREA DFIPVVTWRQ
     LAETCANYLR KGRLAAVEGR IQVRNYENNE GRRVYVTEVI ADNVRFLESP NREGGSQGRD
     EYGGGNGGGN SGGGYGGGGS YGGGNSGGSR SSGSKGGNNQ SDPFADDGKP IDISDDDLPF
//
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