SSB2_SALTY
ID SSB2_SALTY Reviewed; 172 AA.
AC Q93GP7;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Single-stranded DNA-binding protein 2 {ECO:0000255|HAMAP-Rule:MF_00984};
DE Short=SSB 2 {ECO:0000255|HAMAP-Rule:MF_00984};
GN Name=ssb2; OrderedLocusNames=PSLT066;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OG Plasmid pSLT.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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; AE006471; AAL23474.1; -; Genomic_DNA.
DR RefSeq; NP_490554.1; NC_003277.2.
DR RefSeq; WP_000741240.1; NC_003277.2.
DR AlphaFoldDB; Q93GP7; -.
DR SMR; Q93GP7; -.
DR EnsemblBacteria; AAL23474; AAL23474; PSLT066.
DR GeneID; 1256170; -.
DR KEGG; stm:PSLT066; -.
DR PATRIC; fig|99287.12.peg.4926; -.
DR HOGENOM; CLU_078758_0_2_6; -.
DR OMA; GNCIGRF; -.
DR PhylomeDB; Q93GP7; -.
DR BioCyc; SENT99287:PSLT066-MON; -.
DR Proteomes; UP000001014; Plasmid pSLT.
DR GO; GO:0009295; C:nucleoid; IBA:GO_Central.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
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 GO; GO:0051096; P:positive regulation of helicase activity; IBA:GO_Central.
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 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 Plasmid; Reference proteome.
FT CHAIN 1..172
FT /note="Single-stranded DNA-binding protein 2"
FT /id="PRO_0000096093"
FT DOMAIN 6..111
FT /note="SSB"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00984"
FT DNA_BIND 55..61
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00984"
FT REGION 113..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 167..172
FT /note="Important for interaction with partner proteins"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00984"
FT COMPBIAS 113..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 172 AA; 18793 MW; EDA36D294F37AD85 CRC64;
MAARGVNKVI LVGHIGQDPE VRYMPNGGAV ANLTLATSET WRVRQDGEMR EHTEWHRVVV
FGKLAEIASE YLRKGAQVYI EGQLRTRKWT DQSGQDKYTT EVIVNVGGTM QMLGRHNSQP
QQEPQTPPTA AKGEGKAVKG AGNAAKGKNA AAPQQPPAQP DPAYDFDDDI PF
