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Database: UniProt
Entry: A0A143YYH3_9LACT
LinkDB: A0A143YYH3_9LACT
Original site: A0A143YYH3_9LACT 
ID   A0A143YYH3_9LACT        Unreviewed;       180 AA.
AC   A0A143YYH3;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
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=Tpal_2512 {ECO:0000313|EMBL:CZR00391.1};
OS   Trichococcus palustris.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC   Trichococcus.
OX   NCBI_TaxID=140314 {ECO:0000313|EMBL:CZR00391.1, ECO:0000313|Proteomes:UP000242754};
RN   [1] {ECO:0000313|EMBL:CZR00391.1, ECO:0000313|Proteomes:UP000242754}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Trichococcus palustris {ECO:0000313|EMBL:CZR00391.1};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-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; FJNE01000009; CZR00391.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A143YYH3; -.
DR   STRING; 140314.SAMN04488076_10816; -.
DR   OrthoDB; 9809878at2; -.
DR   Proteomes; UP000242754; 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}; Reference proteome {ECO:0000313|Proteomes:UP000242754}.
FT   REGION          104..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           175..180
FT                   /note="Important for interaction with partner proteins"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00984"
FT   COMPBIAS        104..167
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   180 AA;  19901 MW;  EBBFA3710324F57C CRC64;
     MINNVVLVGR LTKDVDLRYT SSGTAVGTFS LAVNRQFTNQ AGEREADFIN CVIWRKAAEN
     FANFTRKGSL VGIEGRIQTR NYENQQGQRV YVTEVVADNF TLLESKNATD QRPRETNTNT
     SGSSANFGSS NSFESNQNRG QVNNQYSAPK QSGFSDFNSN ADPFLSNGES IDISDDDLPF
//
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