ID A0A238JYL9_9RHOB Unreviewed; 173 AA.
AC A0A238JYL9;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-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|RuleBase:RU000524};
DE Short=SSB {ECO:0000256|HAMAP-Rule:MF_00984};
GN Name=ssb_1 {ECO:0000313|EMBL:SMX35761.1};
GN ORFNames=MAA8898_00635 {ECO:0000313|EMBL:SMX35761.1};
OS Maliponia aquimaris.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Maliponia.
OX NCBI_TaxID=1673631 {ECO:0000313|EMBL:SMX35761.1, ECO:0000313|Proteomes:UP000207598};
RN [1] {ECO:0000313|EMBL:SMX35761.1, ECO:0000313|Proteomes:UP000207598}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8898 {ECO:0000313|EMBL:SMX35761.1,
RC ECO:0000313|Proteomes:UP000207598};
RA Song R., Chenine A.L., Ruprecht R.M.;
RL Submitted (MAY-2017) 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; FXYF01000002; SMX35761.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238JYL9; -.
DR OrthoDB; 9809878at2; -.
DR Proteomes; UP000207598; 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|ARBA:ARBA00023172, ECO:0000256|HAMAP-
KW Rule:MF_00984}; DNA repair {ECO:0000256|HAMAP-Rule:MF_00984};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW Rule:MF_00984};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_00984}; Reference proteome {ECO:0000313|Proteomes:UP000207598}.
FT REGION 113..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 168..173
FT /note="Important for interaction with partner proteins"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00984"
SQ SEQUENCE 173 AA; 18840 MW; 01DF19DAD203BD7D CRC64;
MAGSVNKVIL VGNLGRDPEV RTFQNGGKVC NLRIATSENW KDRNTGERRE RTEWHSVAIF
SEPLARIAEQ YLKKGSKVYI EGQLETRKWQ DQSGQDRYST EVVLRPYRSE LTLLDSRDGG
GGGSFGGGSS GGYDDPGQGG GYDDRDYGSS SRSGGGSGPS RAPARDIDDE IPF
//
