SSB1_STRA5
ID SSB1_STRA5 Reviewed; 163 AA.
AC P66851; Q8DXY2; Q8E3K1;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Single-stranded DNA-binding protein 1 {ECO:0000255|HAMAP-Rule:MF_00984};
DE Short=SSB 1 {ECO:0000255|HAMAP-Rule:MF_00984};
GN Name=ssb1; OrderedLocusNames=SAG1713;
OS Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=208435;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-611 / 2603 V/R;
RX PubMed=12200547; DOI=10.1073/pnas.182380799;
RA Tettelin H., Masignani V., Cieslewicz M.J., Eisen J.A., Peterson S.N.,
RA Wessels M.R., Paulsen I.T., Nelson K.E., Margarit I., Read T.D.,
RA Madoff L.C., Wolf A.M., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Lewis M.R., Radune D.,
RA Fedorova N.B., Scanlan D., Khouri H.M., Mulligan S., Carty H.A.,
RA Cline R.T., Van Aken S.E., Gill J., Scarselli M., Mora M., Iacobini E.T.,
RA Brettoni C., Galli G., Mariani M., Vegni F., Maione D., Rinaudo D.,
RA Rappuoli R., Telford J.L., Kasper D.L., Grandi G., Fraser C.M.;
RT "Complete genome sequence and comparative genomic analysis of an emerging
RT human pathogen, serotype V Streptococcus agalactiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(2002).
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:0000255|HAMAP-Rule:MF_00984}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00984}.
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DR EMBL; AE009948; AAN00576.1; -; Genomic_DNA.
DR RefSeq; NP_688703.1; NC_004116.1.
DR RefSeq; WP_000609585.1; NC_004116.1.
DR AlphaFoldDB; P66851; -.
DR SMR; P66851; -.
DR STRING; 208435.SAG1713; -.
DR EnsemblBacteria; AAN00576; AAN00576; SAG1713.
DR GeneID; 66886553; -.
DR KEGG; sag:SAG1713; -.
DR PATRIC; fig|208435.3.peg.1721; -.
DR HOGENOM; CLU_078758_6_2_9; -.
DR OMA; IPVIAWR; -.
DR Proteomes; UP000000821; Chromosome.
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; -; 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 PANTHER; PTHR10302; PTHR10302; 1.
DR Pfam; PF00436; SSB; 1.
DR PIRSF; PIRSF002070; SSB; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR00621; ssb; 1.
DR PROSITE; PS50935; SSB; 1.
PE 3: Inferred from homology;
KW DNA damage; DNA recombination; DNA repair; DNA replication; DNA-binding;
KW Reference proteome.
FT CHAIN 1..163
FT /note="Single-stranded DNA-binding protein 1"
FT /id="PRO_0000096108"
FT DOMAIN 1..104
FT /note="SSB"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00984"
FT REGION 106..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 158..163
FT /note="Important for interaction with partner proteins"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00984"
FT COMPBIAS 106..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 163 AA; 18166 MW; 4DE25F36C8F6E4D2 CRC64;
MINNVVLVGR MTRDAELRYT PSNQAVATFS LAVNRNFKNQ SGEREADFIN CVIWRQQAEN
LANWAKKGAL VGITGRIQTR NYENQQGQRV YVTEVVAESF QLLESRATRE GGSPNSYNNG
GYNNAPSNNS YSASSQQTPN FSRDESPFGN SNPMDISDDD LPF
