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Database: UniProt
Entry: A0A081N9Q7_9GAMM
LinkDB: A0A081N9Q7_9GAMM
Original site: A0A081N9Q7_9GAMM 
ID   A0A081N9Q7_9GAMM        Unreviewed;       198 AA.
AC   A0A081N9Q7;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 40.
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=GZ77_00305 {ECO:0000313|EMBL:KEQ15180.1};
OS   Endozoicomonas montiporae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Endozoicomonadaceae; Endozoicomonas.
OX   NCBI_TaxID=1027273 {ECO:0000313|EMBL:KEQ15180.1, ECO:0000313|Proteomes:UP000028006};
RN   [1] {ECO:0000313|EMBL:KEQ15180.1, ECO:0000313|Proteomes:UP000028006}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 24815 {ECO:0000313|EMBL:KEQ15180.1,
RC   ECO:0000313|Proteomes:UP000028006};
RA   Neave M.J., Apprill A., Voolstra C.R.;
RT   "Whole Genome Sequences of Three Symbiotic Endozoicomonas Bacteria.";
RL   Submitted (JUN-2014) 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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KEQ15180.1}.
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DR   EMBL; JOKG01000001; KEQ15180.1; -; Genomic_DNA.
DR   RefSeq; WP_034872323.1; NZ_JOKG01000001.1.
DR   AlphaFoldDB; A0A081N9Q7; -.
DR   eggNOG; COG0629; Bacteria.
DR   Proteomes; UP000028006; 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:UP000028006}.
FT   DNA_BIND        54..60
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00984"
FT   REGION          111..198
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           193..198
FT                   /note="Important for interaction with partner proteins"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00984"
FT   COMPBIAS        129..178
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   198 AA;  21798 MW;  5B64E1C2C6C7DF65 CRC64;
     MARGVNKVIL IGNLGGDPDV RFTPNGSAVA NFNVATSESW TDKNTGQRQD RTEWHRVVVF
     GKLAEICQQY LRKGSKVYLE GKLQTRKWQD QQGQDRYTTE VVVDGFGGQM QMLDSRQDGG
     MGAVPNQMGG GYQQPQAAPQ QQAPQQQAPQ QRAPQQQYAA PQQQAQPQAQ QRPAPAQQQA
     APQPAAAGFD DFDDDIPF
//
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