ID A0A0B5E162_9RHOB Unreviewed; 134 AA.
AC A0A0B5E162;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=P73_4683 {ECO:0000313|EMBL:AJE49398.1};
OS Celeribacter indicus.
OG Plasmid pP73C {ECO:0000313|EMBL:AJE49398.1,
OG ECO:0000313|Proteomes:UP000031521}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Celeribacter.
OX NCBI_TaxID=1208324 {ECO:0000313|EMBL:AJE49398.1, ECO:0000313|Proteomes:UP000031521};
RN [1] {ECO:0000313|EMBL:AJE49398.1, ECO:0000313|Proteomes:UP000031521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P73 {ECO:0000313|EMBL:AJE49398.1};
RC PLASMID=Plasmid pP73C {ECO:0000313|Proteomes:UP000031521};
RX PubMed=25256706; DOI=10.1099/ijs.0.069039-0;
RA Lai Q., Cao J., Yuan J., Li F., Shao Z.;
RT "Celeribacter indicus sp. nov., a polycyclic aromatic hydrocarbon-degrading
RT bacterium from deep-sea sediment and reclassification of Huaishuia
RT halophila as Celeribacter halophilus comb. nov.";
RL Int. J. Syst. Evol. Microbiol. 64:4160-4167(2014).
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; CP004396; AJE49398.1; -; Genomic_DNA.
DR RefSeq; WP_043872307.1; NZ_FNNW01000063.1.
DR AlphaFoldDB; A0A0B5E162; -.
DR KEGG; cid:P73_4683; -.
DR HOGENOM; CLU_078758_2_2_5; -.
DR OrthoDB; 9809878at2; -.
DR Proteomes; UP000031521; Plasmid pP73C.
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|ARBA:ARBA00023172, ECO:0000256|HAMAP-
KW Rule:MF_00984}; 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}; Plasmid {ECO:0000313|EMBL:AJE49398.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031521}.
FT MOTIF 129..134
FT /note="Important for interaction with partner proteins"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00984"
SQ SEQUENCE 134 AA; 15256 MW; 166A861E872A8566 CRC64;
MQNIVILAGN IGQTPEVRST QSGTKITNFS LATSRPRLSE GRVMRDENGY RVMDTEWHRI
TCFNGLGKTV AEHCEKGMKV LVHGRIHYTK WIDSMGNDRY GCEIIAEKVD FLSRPKSAEN
ENPELVDRDD EIPF
//
