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Database: UniProt
Entry: A0A1I4V6F6_9GAMM
LinkDB: A0A1I4V6F6_9GAMM
Original site: A0A1I4V6F6_9GAMM 
ID   A0A1I4V6F6_9GAMM        Unreviewed;       163 AA.
AC   A0A1I4V6F6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
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=SAMN05216289_101160 {ECO:0000313|EMBL:SFM96745.1};
OS   Dokdonella immobilis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Dokdonella.
OX   NCBI_TaxID=578942 {ECO:0000313|EMBL:SFM96745.1, ECO:0000313|Proteomes:UP000198575};
RN   [1] {ECO:0000313|EMBL:SFM96745.1, ECO:0000313|Proteomes:UP000198575}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.7659 {ECO:0000313|EMBL:SFM96745.1,
RC   ECO:0000313|Proteomes:UP000198575};
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; FOVF01000001; SFM96745.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I4V6F6; -.
DR   STRING; 578942.SAMN05216289_101160; -.
DR   OrthoDB; 9809878at2; -.
DR   Proteomes; UP000198575; 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; 2.
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:UP000198575}.
FT   REGION          107..163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           158..163
FT                   /note="Important for interaction with partner proteins"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00984"
SQ   SEQUENCE   163 AA;  17510 MW;  70C9C5EF0F8C62B9 CRC64;
     MARGVNKVIL VGNLGADPEV KYTAGGTAIC TLSVATSESW KDKQSGEQQE RTEWHRVKLF
     GRLAEIAGEY LKKGRQVYIE GSIRTDKYTD KEGVQRYSTD IIGNEMQMLG GGAEGAGGGG
     GGGNYSRDRG SERSAPRGPQ PGPQRQAAAP ARNDSFEDDD IPF
//
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