ID A0A494YYC8_9BACI Unreviewed; 171 AA.
AC A0A494YYC8;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
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:RKQ15217.1};
GN ORFNames=D8M05_10820 {ECO:0000313|EMBL:RKQ15217.1};
OS Oceanobacillus bengalensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=1435466 {ECO:0000313|EMBL:RKQ15217.1, ECO:0000313|Proteomes:UP000281813};
RN [1] {ECO:0000313|EMBL:RKQ15217.1, ECO:0000313|Proteomes:UP000281813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCCC 1K00260 {ECO:0000313|EMBL:RKQ15217.1,
RC ECO:0000313|Proteomes:UP000281813};
RX PubMed=26303283; DOI=10.1007/s10482-015-0573-5;
RA Yongchang O., Xiang W., Wang G.;
RT "Oceanobacillus bengalensis sp. nov., a bacterium isolated from seawater of
RT the Bay of Bengal.";
RL Antonie Van Leeuwenhoek 108:1189-1196(2015).
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:RKQ15217.1}.
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DR EMBL; RBZO01000015; RKQ15217.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A494YYC8; -.
DR OrthoDB; 9809878at2; -.
DR Proteomes; UP000281813; 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 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|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:UP000281813}.
FT REGION 106..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 166..171
FT /note="Important for interaction with partner proteins"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00984"
FT COMPBIAS 106..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 171 AA; 19277 MW; B05D0DF7D94B6B68 CRC64;
MLNRVVLVGR LTRDPELRYT PTGVAVANFN IAVNRPFTNQ QGNREADFIN GVVWRRQAEN
LANYMKKGNL IGVDGRVQTR NYEGQDGKMV YVTEIVAESI QFLESKGSSG GGQSSLGQNQ
NQFNPNQNQN QNQNQNQFNQ NQFQPNQNQP TEDPFKNNGE PIDISDDDLP F
//
