ID G0JS21_9PROT Unreviewed; 157 AA.
AC G0JS21;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
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=Acife_0300 {ECO:0000313|EMBL:AEM46529.1};
OS Acidithiobacillus ferrivorans SS3.
OC Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=743299 {ECO:0000313|EMBL:AEM46529.1, ECO:0000313|Proteomes:UP000009220};
RN [1] {ECO:0000313|EMBL:AEM46529.1, ECO:0000313|Proteomes:UP000009220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SS3 {ECO:0000313|EMBL:AEM46529.1,
RC ECO:0000313|Proteomes:UP000009220};
RX PubMed=21705598; DOI=10.1128/JB.05373-11;
RA Liljeqvist M., Valdes J., Holmes D.S., Dopson M.;
RT "Draft genome of the psychrotolerant acidophile Acidithiobacillus
RT ferrivorans SS3.";
RL J. Bacteriol. 193:4304-4305(2011).
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}.
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DR EMBL; CP002985; AEM46529.1; -; Genomic_DNA.
DR RefSeq; WP_014027800.1; NC_015942.1.
DR AlphaFoldDB; G0JS21; -.
DR STRING; 743299.Acife_0300; -.
DR KEGG; afi:Acife_0300; -.
DR eggNOG; COG0629; Bacteria.
DR HOGENOM; CLU_078758_0_2_6; -.
DR Proteomes; UP000009220; 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 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:UP000009220}.
FT DNA_BIND 52..58
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00984"
FT REGION 106..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 152..157
FT /note="Important for interaction with partner proteins"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00984"
FT COMPBIAS 125..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 157 AA; 17044 MW; C4AC0A383C9CE0F6 CRC64;
MAGVNKVILL GHLGRDPEMR YQPSGGAIAN FSVATSETFK DKEGNKQERT EWHRVVLFGR
TAEIAGEYLR KGSMAYVEGR LQTRKWTDKE GQERYTTEIV GDRLQLVGAR GGGGGGAASF
DEEDQSRPSG GSSSAGSSRK SEMPPAPAED FDDDIPF
//
