SSBB_BACSU
ID SSBB_BACSU Reviewed; 113 AA.
AC C0SPB6; P94590; Q795B0;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Single-stranded DNA-binding protein B {ECO:0000255|HAMAP-Rule:MF_00984};
DE Short=SSB B {ECO:0000255|HAMAP-Rule:MF_00984};
GN Name=ssbB; Synonyms=ywpH; OrderedLocusNames=BSU36310;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9353933; DOI=10.1099/00221287-143-10-3313;
RA Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V.,
RA Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G.,
RA Kunst F., Danchin A., Glaser P.;
RT "The Bacillus subtilis genome from gerBC (311 degrees) to licR (334
RT degrees).";
RL Microbiology 143:3313-3328(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP SEQUENCE REVISION TO 79.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [4]
RP DEVELOPMENTAL STAGE, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=11918817; DOI=10.1046/j.1365-2958.2002.02833.x;
RA Berka R.M., Hahn J., Albano M., Draskovic I., Persuh M., Cui X., Sloma A.,
RA Widner W., Dubnau D.;
RT "Microarray analysis of the Bacillus subtilis K-state: genome-wide
RT expression changes dependent on ComK.";
RL Mol. Microbiol. 43:1331-1345(2002).
RN [5]
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168 / CU741;
RX PubMed=11948146; DOI=10.1128/jb.184.9.2344-2351.2002;
RA Ogura M., Yamaguchi H., Kobayashi K., Ogasawara N., Fujita Y., Tanaka T.;
RT "Whole-genome analysis of genes regulated by the Bacillus subtilis
RT competence transcription factor ComK.";
RL J. Bacteriol. 184:2344-2351(2002).
RN [6]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=14762004; DOI=10.1128/jb.186.4.1097-1105.2004;
RA Lindner C., Nijland R., van Hartskamp M., Bron S., Hamoen L.W.,
RA Kuipers O.P.;
RT "Differential expression of two paralogous genes of Bacillus subtilis
RT encoding single-stranded DNA binding protein.";
RL J. Bacteriol. 186:1097-1105(2004).
RN [7]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RC STRAIN=168;
RX PubMed=16009133; DOI=10.1016/j.cell.2005.04.035;
RA Hahn J., Maier B., Haijema B.J., Sheetz M., Dubnau D.;
RT "Transformation proteins and DNA uptake localize to the cell poles in
RT Bacillus subtilis.";
RL Cell 122:59-71(2005).
RN [8]
RP PHOSPHORYLATION BY YWQD, AND SUBUNIT.
RC STRAIN=168;
RX PubMed=16549871; DOI=10.1093/nar/gkj514;
RA Mijakovic I., Petranovic D., Macek B., Cepo T., Mann M., Davies J.,
RA Jensen P.R., Vujaklija D.;
RT "Bacterial single-stranded DNA-binding proteins are phosphorylated on
RT tyrosine.";
RL Nucleic Acids Res. 34:1588-1596(2006).
RN [9]
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=17630974; DOI=10.1111/j.1365-2958.2007.05799.x;
RA Kramer N., Hahn J., Dubnau D.;
RT "Multiple interactions among the competence proteins of Bacillus
RT subtilis.";
RL Mol. Microbiol. 65:454-464(2007).
RN [10]
RP FUNCTION.
RX PubMed=25138221; DOI=10.1074/jbc.m114.577924;
RA Yadav T., Carrasco B., Serrano E., Alonso J.C.;
RT "Roles of Bacillus subtilis DprA and SsbA in RecA-mediated genetic
RT recombination.";
RL J. Biol. Chem. 289:27640-27652(2014).
CC -!- FUNCTION: Not essential for replication of the chromosome, but is
CC required for optimal competence (PubMed:14762004). Binds ssDNA, binding
CC is facilitated by DprA, acts as an accessory factor for homologous DNA
CC strand exchange (PubMed:25138221). {ECO:0000269|PubMed:14762004,
CC ECO:0000269|PubMed:25138221}.
CC -!- SUBUNIT: Homotetramer (PubMed:16549871). {ECO:0000255|HAMAP-
CC Rule:MF_00984, ECO:0000269|PubMed:16549871}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16009133,
CC ECO:0000269|PubMed:17630974}. Note=Localizes mostly to the cell poles
CC during the development of competence (PubMed:16009133,
CC PubMed:17630974). Colocalizes with ComGA (PubMed:16009133). During
CC competence a number of proteins (at least CoiA, ComFA, ComGA, DprA,
CC RecA and SsbB) are thought to colocalize at the cell pole
CC (PubMed:17630974). During development of competence ComGA and SsbB
CC colocalize in discrete foci which accumulate at the cell poles and then
CC delocalize without the overall levels of proteins decreasing, these
CC processes are coincident with the timing of transformability and the
CC site of DNA uptake (PubMed:16009133). {ECO:0000269|PubMed:16009133,
CC ECO:0000269|PubMed:17630974}.
CC -!- DEVELOPMENTAL STAGE: Preferentially expressed in cells competent for
CC DNA transformation; that is 5-15% of the population (PubMed:11918817,
CC PubMed:16009133, PubMed:17630974). {ECO:0000269|PubMed:11918817,
CC ECO:0000269|PubMed:16009133, ECO:0000269|PubMed:17630974}.
CC -!- INDUCTION: Only expressed during growth in minimal medium, strongly
CC induced when cells enter stationary phase with highest levels reached
CC about 2 hours after transition to stationary phase (PubMed:14762004).
CC Expression activated by ComK (PubMed:11918817, PubMed:11948146,
CC PubMed:14762004). {ECO:0000269|PubMed:11918817,
CC ECO:0000269|PubMed:11948146, ECO:0000269|PubMed:14762004}.
CC -!- PTM: Phosphorylated by YwqD, which increases ssDNA affinity;
CC dephosphorylated by YwqE. {ECO:0000269|PubMed:16549871}.
CC -!- DISRUPTION PHENOTYPE: Transformation efficiency drops 10- to 50-fold
CC (PubMed:11918817, PubMed:11948146, PubMed:14762004). Destabilization of
CC DprA (PubMed:17630974). {ECO:0000269|PubMed:11918817,
CC ECO:0000269|PubMed:11948146, ECO:0000269|PubMed:14762004,
CC ECO:0000269|PubMed:17630974}.
CC -!- CAUTION: Lacks the C-terminal region present in SsbA and thus is
CC probably not able to participate in DNA replication and/or DNA repair.
CC {ECO:0000305|PubMed:14762004}.
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DR EMBL; Z83337; CAB05949.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15648.2; -; Genomic_DNA.
DR PIR; B70066; B70066.
DR RefSeq; NP_391512.2; NC_000964.3.
DR RefSeq; WP_003227798.1; NZ_JNCM01000034.1.
DR PDB; 3VDY; X-ray; 2.80 A; A/B=1-113.
DR PDBsum; 3VDY; -.
DR AlphaFoldDB; C0SPB6; -.
DR SMR; C0SPB6; -.
DR STRING; 224308.BSU36310; -.
DR PaxDb; C0SPB6; -.
DR EnsemblBacteria; CAB15648; CAB15648; BSU_36310.
DR GeneID; 936910; -.
DR KEGG; bsu:BSU36310; -.
DR PATRIC; fig|224308.179.peg.3930; -.
DR eggNOG; COG0629; Bacteria.
DR InParanoid; C0SPB6; -.
DR OMA; ENTALYC; -.
DR PhylomeDB; C0SPB6; -.
DR BioCyc; BSUB:BSU36310-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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-KW.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR GO; GO:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW.
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 PIRSF; PIRSF002070; SSB; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR00621; ssb; 1.
DR PROSITE; PS50935; SSB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Competence; Cytoplasm; DNA recombination; DNA-binding;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..113
FT /note="Single-stranded DNA-binding protein B"
FT /id="PRO_0000389261"
FT DOMAIN 1..104
FT /note="SSB"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00984"
FT MOD_RES 82
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
FT CONFLICT 79
FT /note="T -> A (in Ref. 1; CAB05949)"
FT /evidence="ECO:0000305"
FT STRAND 5..13
FT /evidence="ECO:0007829|PDB:3VDY"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:3VDY"
FT STRAND 25..34
FT /evidence="ECO:0007829|PDB:3VDY"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:3VDY"
FT STRAND 46..54
FT /evidence="ECO:0007829|PDB:3VDY"
FT HELIX 55..64
FT /evidence="ECO:0007829|PDB:3VDY"
FT STRAND 70..82
FT /evidence="ECO:0007829|PDB:3VDY"
FT STRAND 90..102
FT /evidence="ECO:0007829|PDB:3VDY"
SQ SEQUENCE 113 AA; 12520 MW; 0B475176EC4CB55B CRC64;
MFNQVMLVGR LTKDPDLRYT SAGAAVAHVT LAVNRSFKNA SGEIEADYVN CTLWRKTAEN
TALYCQKGSL VGVSGRIQTR SYENEEGVNV YVTEVLADTV RFMDPKPREK AAD
