ID Q4FLZ6_PELUB Unreviewed; 152 AA.
AC Q4FLZ6;
DT 30-AUG-2005, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2005, sequence version 1.
DT 27-MAR-2024, entry version 113.
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 Name=ssb {ECO:0000313|EMBL:AAZ21792.1};
GN OrderedLocusNames=SAR11_0984 {ECO:0000313|EMBL:AAZ21792.1};
OS Pelagibacter ubique (strain HTCC1062).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Candidatus Pelagibacterales;
OC Candidatus Pelagibacteraceae; Pelagibacter.
OX NCBI_TaxID=335992 {ECO:0000313|EMBL:AAZ21792.1, ECO:0000313|Proteomes:UP000002528};
RN [1] {ECO:0000313|EMBL:AAZ21792.1, ECO:0000313|Proteomes:UP000002528}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC1062 {ECO:0000313|EMBL:AAZ21792.1,
RC ECO:0000313|Proteomes:UP000002528};
RX PubMed=16109880; DOI=10.1126/science.1114057;
RA Giovannoni S.J., Tripp H.J., Givan S., Podar M., Vergin K.L., Baptista D.,
RA Bibbs L., Eads J., Richardson T.H., Noordewier M., Rappe M.S., Short J.M.,
RA Carrington J.C., Mathur E.J.;
RT "Genome streamlining in a cosmopolitan oceanic bacterium.";
RL Science 309:1242-1245(2005).
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; CP000084; AAZ21792.1; -; Genomic_DNA.
DR RefSeq; WP_011282083.1; NC_007205.1.
DR AlphaFoldDB; Q4FLZ6; -.
DR STRING; 335992.SAR11_0984; -.
DR KEGG; pub:SAR11_0984; -.
DR eggNOG; COG0629; Bacteria.
DR HOGENOM; CLU_078758_0_2_5; -.
DR OrthoDB; 9809878at2; -.
DR Proteomes; UP000002528; 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|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:UP000002528}.
FT DNA_BIND 54..60
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00984"
FT REGION 116..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 147..152
FT /note="Important for interaction with partner proteins"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00984"
FT COMPBIAS 116..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 152 AA; 16696 MW; 9C38872CAAB1A01A CRC64;
MAGSLNKVLL IGRLGADPEI KQMVNGKSVA RLSLATSQSW KDKTTGEKKE KTEWHRIVVF
NDGLVNVVQQ YLKKGAQIYV EGQIATRKWK DEQSGQDKYS TEIVIQGYNS SLTMLGGGNT
GGGIQNDNTQ GPANNFEDSP QTSNDMDDEI PF
//
