ID A0A2H5F3L5_9RHOB Unreviewed; 173 AA.
AC A0A2H5F3L5;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Single-stranded DNA-binding protein {ECO:0000256|HAMAP-Rule:MF_00984, ECO:0000256|RuleBase:RU000524};
DE Short=SSB {ECO:0000256|HAMAP-Rule:MF_00984};
GN ORFNames=CX676_02480 {ECO:0000313|EMBL:AUH66117.1};
OS Paracoccus zhejiangensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=1077935 {ECO:0000313|EMBL:AUH66117.1, ECO:0000313|Proteomes:UP000234530};
RN [1] {ECO:0000313|EMBL:AUH66117.1, ECO:0000313|Proteomes:UP000234530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J6 {ECO:0000313|EMBL:AUH66117.1,
RC ECO:0000313|Proteomes:UP000234530};
RX PubMed=23653121; DOI=10.1007/s10482-013-9932-2;
RA Wu Z.G., Zhang D.F., Liu Y.L., Wang F., Jiang X., Li C., Li S.P., Hong Q.,
RA Li W.J.;
RT "Paracoccus zhejiangensis sp. nov., isolated from activated sludge in
RT wastewater-treatment system.";
RL Antonie Van Leeuwenhoek 104:123-128(2013).
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; CP025430; AUH66117.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H5F3L5; -.
DR KEGG; pzh:CX676_02480; -.
DR OrthoDB; 9809878at2; -.
DR Proteomes; UP000234530; 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 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:UP000234530}.
FT REGION 111..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 168..173
FT /note="Important for interaction with partner proteins"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00984"
SQ SEQUENCE 173 AA; 18354 MW; 3F331C69BAA062EE CRC64;
MAGSVNKVIL IGNLGQDPEV RTFQNGGKVV NLRIATSEQW KDRNSGERQE RTQWHSVAIF
SEPLARIAEQ YLKKGSKVYL EGQLETRKWQ DQSGQDRYTT EVVLRPFSGN LTLLDGRGEG
GGGGGGNYGG GSRGGSGGGY DDRGGYDQGP SSGGGSSSGG SGGRSDYDDE IPF
//
