SSBA_BACSU
ID SSBA_BACSU Reviewed; 172 AA.
AC P37455;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Single-stranded DNA-binding protein A {ECO:0000255|HAMAP-Rule:MF_00984};
DE Short=SSB A {ECO:0000255|HAMAP-Rule:MF_00984};
GN Name=ssbA; OrderedLocusNames=BSU40900;
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=7584024; DOI=10.1093/dnares/1.1.1;
RA Ogasawara N., Nakai S., Yoshikawa H.;
RT "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT chromosome containing the replication origin.";
RL DNA Res. 1:1-14(1994).
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 INDUCTION.
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 [4]
RP PHOSPHORYLATION AT TYR-82, SUBUNIT, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
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 [5]
RP FUNCTION, INTERACTION WITH PARTNER PROTEINS, AND DNA-BINDING.
RX PubMed=21170359; DOI=10.1371/journal.pgen.1001238;
RA Costes A., Lecointe F., McGovern S., Quevillon-Cheruel S., Polard P.;
RT "The C-terminal domain of the bacterial SSB protein acts as a DNA
RT maintenance hub at active chromosome replication forks.";
RL PLoS Genet. 6:E1001238-E1001238(2010).
RN [6]
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: 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 (PubMed:21170359).
CC Has a 20-fold higher affinity for ssDNA than SsbB; SsbA and DprA
CC activate the homologous DNA strand exchange function of RecA-ATP
CC (PubMed:25138221). {ECO:0000269|PubMed:25138221,
CC ECO:0000305|PubMed:21170359}.
CC -!- SUBUNIT: Homotetramer. Interacts with several proteins involved in DNA
CC metabolism such as PriA, RecQ, RecG, RecS, DnaE, RarA, RecJ, RecO,
CC SbcC, YrrC, XseA and Ung. {ECO:0000255|HAMAP-Rule:MF_00984,
CC ECO:0000269|PubMed:16549871, ECO:0000269|PubMed:21170359}.
CC -!- INDUCTION: Strongly expressed during exponential growth, decreases 2-4-
CC fold in stationary phase, part of the rpsF-ssbA-rpsR and the ychF-rpsF-
CC ssbA-rpsR operons (PubMed:14762004). The operon is induced by DNA
CC damage by mitomycin C (PubMed:14762004). {ECO:0000269|PubMed:14762004}.
CC -!- PTM: Phosphorylated by YwqD, which increases ssDNA affinity;
CC dephosphorylated by YwqE. {ECO:0000269|PubMed:16549871}.
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DR EMBL; D26185; BAA05220.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB16127.1; -; Genomic_DNA.
DR PIR; S66014; S66014.
DR RefSeq; NP_391970.1; NC_000964.3.
DR RefSeq; WP_003219228.1; NZ_JNCM01000034.1.
DR PDB; 6BHW; X-ray; 2.21 A; A/B/C/D/E/F/G/H=1-116.
DR PDB; 6BHX; X-ray; 2.94 A; A/B/C/D=1-116.
DR PDBsum; 6BHW; -.
DR PDBsum; 6BHX; -.
DR AlphaFoldDB; P37455; -.
DR SMR; P37455; -.
DR IntAct; P37455; 1.
DR STRING; 224308.BSU40900; -.
DR iPTMnet; P37455; -.
DR jPOST; P37455; -.
DR PaxDb; P37455; -.
DR PRIDE; P37455; -.
DR EnsemblBacteria; CAB16127; CAB16127; BSU_40900.
DR GeneID; 64305876; -.
DR GeneID; 937911; -.
DR KEGG; bsu:BSU40900; -.
DR PATRIC; fig|224308.179.peg.4431; -.
DR eggNOG; COG0629; Bacteria.
DR InParanoid; P37455; -.
DR OMA; GQMQERT; -.
DR PhylomeDB; P37455; -.
DR BioCyc; BSUB:BSU40900-MON; -.
DR Proteomes; UP000001570; Chromosome.
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 DisProt; DP02196; -.
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 1: Evidence at protein level;
KW 3D-structure; DNA damage; DNA recombination; DNA repair; DNA replication;
KW DNA-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..172
FT /note="Single-stranded DNA-binding protein A"
FT /id="PRO_0000096005"
FT DOMAIN 1..104
FT /note="SSB"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00984"
FT REGION 103..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..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 82
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:16549871"
FT STRAND 2..13
FT /evidence="ECO:0007829|PDB:6BHW"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:6BHW"
FT STRAND 25..34
FT /evidence="ECO:0007829|PDB:6BHW"
FT STRAND 46..54
FT /evidence="ECO:0007829|PDB:6BHW"
FT HELIX 56..64
FT /evidence="ECO:0007829|PDB:6BHW"
FT STRAND 70..79
FT /evidence="ECO:0007829|PDB:6BHW"
FT STRAND 93..102
FT /evidence="ECO:0007829|PDB:6BHW"
SQ SEQUENCE 172 AA; 18742 MW; C170025FBDACDC5D CRC64;
MLNRVVLVGR LTKDPELRYT PNGAAVATFT LAVNRTFTNQ SGEREADFIN CVTWRRQAEN
VANFLKKGSL AGVDGRLQTR NYENQQGQRV FVTEVQAESV QFLEPKNGGG SGSGGYNEGN
SGGGQYFGGG QNDNPFGGNQ NNQRRNQGNS FNDDPFANDG KPIDISDDDL PF
