ID A0A370GB07_9BACI Unreviewed; 177 AA.
AC A0A370GB07;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=DFR59_11126 {ECO:0000313|EMBL:RDI40887.1};
OS Falsibacillus pallidus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Falsibacillus.
OX NCBI_TaxID=493781 {ECO:0000313|EMBL:RDI40887.1, ECO:0000313|Proteomes:UP000255326};
RN [1] {ECO:0000313|EMBL:RDI40887.1, ECO:0000313|Proteomes:UP000255326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25281 {ECO:0000313|EMBL:RDI40887.1,
RC ECO:0000313|Proteomes:UP000255326};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (JUL-2018) 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:RDI40887.1}.
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DR EMBL; QQAY01000011; RDI40887.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A370GB07; -.
DR Proteomes; UP000255326; 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:UP000255326}.
FT REGION 105..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 172..177
FT /note="Important for interaction with partner proteins"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00984"
FT COMPBIAS 106..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 177 AA; 19921 MW; 56AE5159FB6575C2 CRC64;
MILMMNRVIL VGRLTKDPEL RYTPSGVAVA TFTLAVNRSF TNQQGEREAD FINCVIWRRP
AENVANFLKK GSLAGVDGRI QTRNYEGQDG RKVYVTEVMA ESVQFLEPKN ANNQDRGNAS
SSGGGNQRNQ DYPFNQNQNQ NQNQRSNNNN QGYTRLDEDP FANDGQPIDI SDDDLPF
//
