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Database: UniProt
Entry: A0A2S0VQK9_9ALTE
LinkDB: A0A2S0VQK9_9ALTE
Original site: A0A2S0VQK9_9ALTE 
ID   A0A2S0VQK9_9ALTE        Unreviewed;       206 AA.
AC   A0A2S0VQK9;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
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=C2869_08700 {ECO:0000313|EMBL:AWB66501.1};
OS   Saccharobesus litoralis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Saccharobesus.
OX   NCBI_TaxID=2172099 {ECO:0000313|EMBL:AWB66501.1, ECO:0000313|Proteomes:UP000244441};
RN   [1] {ECO:0000313|EMBL:AWB66501.1, ECO:0000313|Proteomes:UP000244441}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCB-QB4 {ECO:0000313|EMBL:AWB66501.1,
RC   ECO:0000313|Proteomes:UP000244441};
RA   Tan W.R., Lau N.-S., Go F., Amirul A.-A.A.;
RT   "Genome sequence of a Cantenovulum-like bacteria.";
RL   Submitted (JAN-2018) 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; CP026604; AWB66501.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S0VQK9; -.
DR   KEGG; cate:C2869_08700; -.
DR   OrthoDB; 9809878at2; -.
DR   Proteomes; UP000244441; Chromosome.
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:UP000244441}.
FT   REGION          112..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           201..206
FT                   /note="Important for interaction with partner proteins"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00984"
FT   COMPBIAS        120..181
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        182..196
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   206 AA;  22654 MW;  40668B2230AE15E9 CRC64;
     MARGINKVIL IGNLGQDPEV RYFPNGGAIC NVTVATTESW KDRQSGEQRE STEWHRVVFN
     NRLAEIAGEY LRKGSKVYVE GSLRTRKWQN QQGQDQYTTE IRANEMQMLD ARGGQEGGYQ
     PRPQGQQAGY QPQAAAPQAQ GGYQPQQSSQ PQQAAQPQQS AQPQYQPQQS AGYQPSSAPA
     QPAAAPSTPP PAPVEPNIDF DDDIPF
//
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