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Database: UniProt
Entry: A0A0W7U4B5_9GAMM
LinkDB: A0A0W7U4B5_9GAMM
Original site: A0A0W7U4B5_9GAMM 
ID   A0A0W7U4B5_9GAMM        Unreviewed;       186 AA.
AC   A0A0W7U4B5;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 43.
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=ATO46_14555 {ECO:0000313|EMBL:KUE80939.1};
OS   Aeromonas schubertii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=652 {ECO:0000313|EMBL:KUE80939.1, ECO:0000313|Proteomes:UP000054876};
RN   [1] {ECO:0000313|EMBL:KUE80939.1, ECO:0000313|Proteomes:UP000054876}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43700 {ECO:0000313|EMBL:KUE80939.1,
RC   ECO:0000313|Proteomes:UP000054876};
RA   Liu L., Li Q., Zhang F., Shi B.;
RT   "Complete genome sequence of Aeromonas schubertii strain ATCC43700.";
RL   Submitted (DEC-2015) 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}.
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:KUE80939.1}.
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DR   EMBL; LPUO01000006; KUE80939.1; -; Genomic_DNA.
DR   RefSeq; WP_050667861.1; NZ_LPUO01000006.1.
DR   AlphaFoldDB; A0A0W7U4B5; -.
DR   STRING; 652.WL1483_2168; -.
DR   OrthoDB; 9809878at2; -.
DR   Proteomes; UP000054876; 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          113..186
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           181..186
FT                   /note="Important for interaction with partner proteins"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00984"
FT   COMPBIAS        124..163
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   186 AA;  20529 MW;  9BDCCDDD67533F24 CRC64;
     MASRGINKVI LIGNLGQDPE VRYMPSGGAV TNITLATSET WRDKQTGEQK ERTEWHRVVF
     MGKLAEVAGE YLRKGSQVYV EGKLQTRKWQ DQSGQERYTT EVLVDSFTGV MQMLGGRPQG
     AGQPMNQGGG QQGWGQPQQP MQQASRPAPS QGMQQQGGYS RPAAQPQSAP PVYNEPPMDF
     DDDIPF
//
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