ID A0A329MI34_9BACL Unreviewed; 159 AA.
AC A0A329MI34;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=DQG23_21110 {ECO:0000313|EMBL:RAV19489.1};
OS Paenibacillus contaminans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=450362 {ECO:0000313|EMBL:RAV19489.1, ECO:0000313|Proteomes:UP000250369};
RN [1] {ECO:0000313|EMBL:RAV19489.1, ECO:0000313|Proteomes:UP000250369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CKOBP-6 {ECO:0000313|EMBL:RAV19489.1,
RC ECO:0000313|Proteomes:UP000250369};
RX PubMed=19126735; DOI=10.1099/ijs.0.001495-0;
RA Chou J.H., Lee J.H., Lin M.C., Chang P.S., Arun A.B., Young C.C.,
RA Chen W.M.;
RT "Paenibacillus contaminans sp. nov., isolated from a contaminated
RT laboratory plate.";
RL Int. J. Syst. Evol. Microbiol. 59:125-129(2009).
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:RAV19489.1}.
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DR EMBL; QMFB01000012; RAV19489.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A329MI34; -.
DR OrthoDB; 9809878at2; -.
DR Proteomes; UP000250369; 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:UP000250369}.
FT REGION 106..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 154..159
FT /note="Important for interaction with partner proteins"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00984"
SQ SEQUENCE 159 AA; 17724 MW; 63483F850DFCD855 CRC64;
MLNRVILIGR LTRDPELRYT PAGVAVTQFT LAVDRPFSNQ QKEREADFIP VVVWRQQAEH
CANYLRKGRL AAVEGRMQVR NYDNNEGRKV YVTEVVADNV RFLESANSQN QGGGGGAARD
EFAPPAPSQN RSFGGARNNQ DPFSDDGKPI DISDDDLPF
//
