ID A0A1M4XC05_9FIRM Unreviewed; 146 AA.
AC A0A1M4XC05;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=SAMN02745190_01429 {ECO:0000313|EMBL:SHE90950.1};
OS Schwartzia succinivorans DSM 10502.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Schwartzia.
OX NCBI_TaxID=1123243 {ECO:0000313|EMBL:SHE90950.1, ECO:0000313|Proteomes:UP000184404};
RN [1] {ECO:0000313|EMBL:SHE90950.1, ECO:0000313|Proteomes:UP000184404}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10502 {ECO:0000313|EMBL:SHE90950.1,
RC ECO:0000313|Proteomes:UP000184404};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FQUG01000005; SHE90950.1; -; Genomic_DNA.
DR RefSeq; WP_072935522.1; NZ_FQUG01000005.1.
DR AlphaFoldDB; A0A1M4XC05; -.
DR STRING; 1123243.SAMN02745190_01429; -.
DR OrthoDB; 9809878at2; -.
DR Proteomes; UP000184404; 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|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:UP000184404}.
FT REGION 104..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 141..146
FT /note="Important for interaction with partner proteins"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00984"
SQ SEQUENCE 146 AA; 16011 MW; 6ED95AD834F6031F CRC64;
MNKVILMGRL ARDPDVRSTQ SGKSVARMTI AVDRRVSRNA QPGQPTADFL NLVAWERMAE
FCQNYLRKGT KILVEGRLQS RSYEAQDGSK RYVTEVSVTD IEFAESKSHD SSGGQNFVGG
QFDAPPAAQG PQQGFGGPVT DDDIPF
//
