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Database: UniProt
Entry: U7UQ98_9FIRM
LinkDB: U7UQ98_9FIRM
Original site: U7UQ98_9FIRM 
ID   U7UQ98_9FIRM            Unreviewed;       144 AA.
AC   U7UQ98;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 51.
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:ERT61495.1};
GN   ORFNames=HMPREF1250_0520 {ECO:0000313|EMBL:ERT61495.1};
OS   Megasphaera vaginalis.
OC   Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC   Megasphaera.
OX   NCBI_TaxID=1111454 {ECO:0000313|EMBL:ERT61495.1, ECO:0000313|Proteomes:UP000017090};
RN   [1] {ECO:0000313|EMBL:ERT61495.1, ECO:0000313|Proteomes:UP000017090}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BV3C16-1 {ECO:0000313|EMBL:ERT61495.1,
RC   ECO:0000313|Proteomes:UP000017090};
RA   Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA   Methe B., Sutton G., Nelson K.E.;
RL   Submitted (SEP-2013) 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:ERT61495.1}.
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DR   EMBL; AWXA01000009; ERT61495.1; -; Genomic_DNA.
DR   RefSeq; WP_023053146.1; NZ_AWXA01000009.1.
DR   AlphaFoldDB; U7UQ98; -.
DR   STRING; 1111454.HMPREF1250_0520; -.
DR   PATRIC; fig|1111454.3.peg.634; -.
DR   eggNOG; COG0629; Bacteria.
DR   OrthoDB; 9809878at2; -.
DR   Proteomes; UP000017090; 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:SF0; SINGLE-STRANDED DNA-BINDING PROTEIN, MITOCHONDRIAL; 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:UP000017090}.
FT   REGION          109..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           139..144
FT                   /note="Important for interaction with partner proteins"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00984"
FT   COMPBIAS        109..133
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   144 AA;  15448 MW;  357F9E735791F636 CRC64;
     MNSVQLMGNL ARDPEIRFTK TGKAVARFTV ACTRTYVPAG SQEQRELTDF IPCVAWGNLA
     ESCGNNLAKG SRVFVEGRIS VRSYETAEGQ KRYVTEVVAD FVGQTLGSDS RQFSAQPASP
     QQGPASSGSG FDGLGSDSDE EIPF
//
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