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Database: UniProt
Entry: A0A1M6Z095_9FLAO
LinkDB: A0A1M6Z095_9FLAO
Original site: A0A1M6Z095_9FLAO 
ID   A0A1M6Z095_9FLAO        Unreviewed;       149 AA.
AC   A0A1M6Z095;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
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=SAMN05443634_107110 {ECO:0000313|EMBL:SHL23785.1};
OS   Chishuiella changwenlii.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Chishuiella.
OX   NCBI_TaxID=1434701 {ECO:0000313|EMBL:SHL23785.1, ECO:0000313|Proteomes:UP000184120};
RN   [1] {ECO:0000313|Proteomes:UP000184120}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27989 {ECO:0000313|Proteomes:UP000184120};
RA   Varghese N., Submissions S.;
RL   Submitted (NOV-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; FRBH01000007; SHL23785.1; -; Genomic_DNA.
DR   RefSeq; WP_072932246.1; NZ_FRBH01000007.1.
DR   AlphaFoldDB; A0A1M6Z095; -.
DR   STRING; 1434701.SAMN05443634_107110; -.
DR   OrthoDB; 9809878at2; -.
DR   Proteomes; UP000184120; 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}.
FT   REGION          109..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..135
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   149 AA;  17053 MW;  880B73238972BEFE CRC64;
     MNGTTNKVLL IGNLGDDVKL HNFDEQNCIG RFPIATTESY ISRTGERITE TEWHNIVTRN
     KLAELCDRYL KKGDKVFVEG RIKTRKWDDN GQTRYTTEIV ANSIEFLTPK VENENRQSTQ
     EDSNKTASSQ NTPIVEPPFI EDGEDDLPF
//
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