ID E2ZNS8_9FIRM Unreviewed; 154 AA.
AC E2ZNS8;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 64.
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 ORFNames=HMPREF9436_03359 {ECO:0000313|EMBL:EFQ05171.1};
OS Faecalibacterium cf. prausnitzii KLE1255.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Faecalibacterium.
OX NCBI_TaxID=748224 {ECO:0000313|EMBL:EFQ05171.1, ECO:0000313|Proteomes:UP000006028};
RN [1] {ECO:0000313|EMBL:EFQ05171.1, ECO:0000313|Proteomes:UP000006028}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KLE1255 {ECO:0000313|EMBL:EFQ05171.1,
RC ECO:0000313|Proteomes:UP000006028};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2010) 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:EFQ05171.1}.
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DR EMBL; AECU01000248; EFQ05171.1; -; Genomic_DNA.
DR RefSeq; WP_005946586.1; NZ_GL538351.1.
DR AlphaFoldDB; E2ZNS8; -.
DR STRING; 748224.HMPREF9436_03359; -.
DR eggNOG; COG0629; Bacteria.
DR HOGENOM; CLU_078758_6_2_9; -.
DR OrthoDB; 9809878at2; -.
DR BioCyc; FCF748224-HMP:GTSS-2331-MONOMER; -.
DR Proteomes; UP000006028; 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 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}.
FT REGION 104..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 149..154
FT /note="Important for interaction with partner proteins"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00984"
FT COMPBIAS 104..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 154 AA; 17030 MW; 059CE48139EC7CB3 CRC64;
MLNMIAIMGR LTNTPELRTT TSGKEVCSFD IACERSYSAN GQRETDFLPC VAWGKTAQFV
SQYFDKGSMI AVNGSLQTRK YQDKQGNNRT AYEIQVREVS FCGSKAPDST STRGFDEQTE
SYASEARNAQ SAQQAAETGT DDFAVINDDE DLPF
//