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Database: UniProt
Entry: A0A0L6CXE6_9RHOB
LinkDB: A0A0L6CXE6_9RHOB
Original site: A0A0L6CXE6_9RHOB 
ID   A0A0L6CXE6_9RHOB        Unreviewed;       167 AA.
AC   A0A0L6CXE6;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
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   Name=ssb {ECO:0000313|EMBL:KNX42437.1};
GN   ORFNames=ROTO_09460 {ECO:0000313|EMBL:KNX42437.1};
OS   Roseovarius tolerans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseovarius.
OX   NCBI_TaxID=74031 {ECO:0000313|EMBL:KNX42437.1, ECO:0000313|Proteomes:UP000037046};
RN   [1] {ECO:0000313|Proteomes:UP000037046}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EL-164 {ECO:0000313|Proteomes:UP000037046};
RA   Voget S., Bruns H., Wagner-Doebler I., Schulz S., Daniel R.;
RT   "Draft Genome Sequence of Roseovarius tolerans EL-164, a producer of N-
RT   Acylated Alanine Methyl Esters (NAMEs).";
RL   Submitted (JUL-2015) 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}.
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:KNX42437.1}.
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DR   EMBL; LGVV01000008; KNX42437.1; -; Genomic_DNA.
DR   RefSeq; WP_050661879.1; NZ_LGVV01000008.1.
DR   AlphaFoldDB; A0A0L6CXE6; -.
DR   STRING; 74031.SAMN04488077_10296; -.
DR   PATRIC; fig|74031.6.peg.969; -.
DR   OrthoDB; 9809878at2; -.
DR   Proteomes; UP000037046; 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   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:UP000037046}.
FT   REGION          114..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           162..167
FT                   /note="Important for interaction with partner proteins"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00984"
SQ   SEQUENCE   167 AA;  17990 MW;  08EFAE010C7EA352 CRC64;
     MAGSVNKVII IGNLGRDPEV RTFQNGGKVC NLRIATSENW KDRNTGERRE RTEWHTVAIF
     NEALVRLAEQ YLKKGSKVYI EGKLETRKWQ DQSGQDRYST EVVLRPYAGE MTFLDGRSDG
     GGGGGGGGSY GGGQDQGYGG GDYGGGSDAG GGGDSRPSRD MDDEIPF
//
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