ID A0A1I0VWG9_9BACT Unreviewed; 153 AA.
AC A0A1I0VWG9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=SAMN04489723_101410 {ECO:0000313|EMBL:SFA80538.1};
OS Algoriphagus aquimarinus.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Algoriphagus.
OX NCBI_TaxID=237018 {ECO:0000313|EMBL:SFA80538.1, ECO:0000313|Proteomes:UP000198790};
RN [1] {ECO:0000313|EMBL:SFA80538.1, ECO:0000313|Proteomes:UP000198790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23399 {ECO:0000313|EMBL:SFA80538.1,
RC ECO:0000313|Proteomes:UP000198790};
RA de Groot N.N.;
RL Submitted (OCT-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; FOKK01000001; SFA80538.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0VWG9; -.
DR STRING; 237018.SAMN04489723_101410; -.
DR OrthoDB; 9809878at2; -.
DR Proteomes; UP000198790; 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:SF0; SINGLE-STRANDED DNA-BINDING PROTEIN, MITOCHONDRIAL; 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:UP000198790}.
FT REGION 106..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 148..153
FT /note="Important for interaction with partner proteins"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00984"
FT COMPBIAS 115..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 153 AA; 16959 MW; CC55799B7E8BD3E0 CRC64;
MAGVNKVILV GNLGADPEVK YLEGDNTVAN LRLATTEAYK NRNGERVEQT EWHDLEMWGA
QAKIAEQYLK KGSQIYVEGK IKTDSWQDEQ GQNRYRTRIR VLSFTMLGSK PDGAGNPSAP
QQSTQQRPAS SAPTSAPKAQ EMVSDTEDDD LPF
//
