CSPB_BACSU
ID CSPB_BACSU Reviewed; 67 AA.
AC P32081; P41017; Q45690;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Cold shock protein CspB;
DE AltName: Full=Major cold shock protein;
GN Name=cspB; Synonyms=cspA; OrderedLocusNames=BSU09100;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1400185; DOI=10.1128/jb.174.20.6326-6335.1992;
RA Willimsky G., Bang H., Fisher G., Marahiel M.A.;
RT "Characterization of cspB, a Bacillus subtilis inducible cold shock gene
RT affecting cell viability at low temperatures.";
RL J. Bacteriol. 174:6326-6335(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / JH642;
RA Wendrich T.M., Marahiel M.A.;
RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969498; DOI=10.1099/13500872-142-11-3021;
RA Noback M.A., Terpstra P., Holsappel S., Venema G., Bron S.;
RT "A 22 kb DNA sequence in the cspB-glpPFKD region at 75 degrees on the
RT Bacillus subtilis chromosome.";
RL Microbiology 142:3021-3026(1996).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 6-62.
RC STRAIN=Globigii;
RX PubMed=8294017; DOI=10.1016/0378-1119(93)90479-m;
RA Schroeder K., Zuber P., Willimsky G., Wagner B., Marahiel M.A.;
RT "Mapping of the Bacillus subtilis cspB gene and cloning of its homologs in
RT thermophilic, mesophilic and psychrotrophic bacilli.";
RL Gene 136:277-280(1993).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 12-56.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=9439003; DOI=10.1038/sj.jim.2900463;
RA Francis K.P., Stewart G.S.A.B.;
RT "Detection and speciation of bacteria through PCR using universal major
RT cold-shock protein primer oligomers.";
RL J. Ind. Microbiol. Biotechnol. 19:286-293(1997).
RN [7]
RP PROTEIN SEQUENCE OF 1-31.
RC STRAIN=168 / JH642;
RX PubMed=8755892; DOI=10.1128/jb.178.15.4611-4619.1996;
RA Graumann P., Schroeder K., Schmid R., Marahiel M.A.;
RT "Cold shock stress-induced proteins in Bacillus subtilis.";
RL J. Bacteriol. 178:4611-4619(1996).
RN [8]
RP FUNCTION.
RX PubMed=8307174; DOI=10.1016/0014-5793(94)80355-2;
RA Graumann P., Marahiel M.A.;
RT "The major cold shock protein of Bacillus subtilis CspB binds with high
RT affinity to the ATTGG- and CCAAT sequences in single stranded
RT oligonucleotides.";
RL FEBS Lett. 338:157-160(1994).
RN [9]
RP INTERACTION WITH CSHB, SUBUNIT, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=168 / JH642;
RX PubMed=16352840; DOI=10.1128/jb.188.1.240-248.2006;
RA Hunger K., Beckering C.L., Wiegeshoff F., Graumann P.L., Marahiel M.A.;
RT "Cold-induced putative DEAD box RNA helicases CshA and CshB are essential
RT for cold adaptation and interact with cold shock protein B in Bacillus
RT subtilis.";
RL J. Bacteriol. 188:240-248(2006).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=8321288; DOI=10.1038/364164a0;
RA Schindelin H., Marahiel M.A., Heinemann U.;
RT "Universal nucleic acid-binding domain revealed by crystal structure of the
RT B. subtilis major cold-shock protein.";
RL Nature 364:164-168(1993).
RN [11]
RP STRUCTURE BY NMR.
RX PubMed=8321289; DOI=10.1038/364169a0;
RA Schnuchel A., Wiltscheck R., Czisch M., Herrier M., Willimsky G.,
RA Graumann P., Marahiel M.A., Holak T.A.;
RT "Structure in solution of the major cold-shock protein from Bacillus
RT subtilis.";
RL Nature 364:169-171(1993).
CC -!- FUNCTION: Binds to the pentamer sequences ATTGG and CCAAT with highest
CC affinity in single-stranded DNA, and also to other sequences. Has
CC greater affinity for ATTGG than CCAAT. Can act as transcriptional
CC activator of cold shock genes by recognizing putative ATTGG-box
CC elements present in promoter regions of genes induced under cold shock
CC conditions. {ECO:0000269|PubMed:8307174}.
CC -!- SUBUNIT: Homodimer. Interacts with RNA helicase CshB when cells are
CC transcriptionally active. {ECO:0000269|PubMed:16352840}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid
CC {ECO:0000269|PubMed:16352840}. Note=Shows transcription-dependent
CC localization at subcellular sites surrounding the nucleoid.
CC -!- INDUCTION: In response to low temperature.
CC -!- DISRUPTION PHENOTYPE: A double cshB-cspB disruption mutant cannot be
CC made. {ECO:0000269|PubMed:16352840}.
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DR EMBL; X59715; CAA42235.1; -; Genomic_DNA.
DR EMBL; U58859; AAB01346.1; -; Genomic_DNA.
DR EMBL; X96983; CAA65693.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12738.1; -; Genomic_DNA.
DR EMBL; U60029; AAC80233.1; -; Genomic_DNA.
DR EMBL; U60030; AAC80234.1; -; Genomic_DNA.
DR EMBL; X73463; CAA51842.1; -; Genomic_DNA.
DR PIR; A45723; A45723.
DR RefSeq; NP_388791.1; NC_000964.3.
DR RefSeq; WP_003224086.1; NZ_JNCM01000035.1.
DR PDB; 1CSP; X-ray; 2.45 A; A=1-67.
DR PDB; 1CSQ; X-ray; 2.70 A; A=1-67.
DR PDB; 1NMF; NMR; -; A=1-67.
DR PDB; 1NMG; NMR; -; A=1-67.
DR PDB; 2ES2; X-ray; 1.78 A; A=1-67.
DR PDB; 2F52; NMR; -; A=1-67.
DR PDB; 2I5L; X-ray; 2.55 A; X=1-67.
DR PDB; 2I5M; X-ray; 2.30 A; X=1-67.
DR PDB; 3PF4; X-ray; 1.38 A; A/B=1-67.
DR PDB; 3PF5; X-ray; 1.68 A; A/B=1-67.
DR PDB; 6SZZ; X-ray; 2.05 A; A=1-67.
DR PDB; 6T00; X-ray; 2.10 A; A=1-66.
DR PDBsum; 1CSP; -.
DR PDBsum; 1CSQ; -.
DR PDBsum; 1NMF; -.
DR PDBsum; 1NMG; -.
DR PDBsum; 2ES2; -.
DR PDBsum; 2F52; -.
DR PDBsum; 2I5L; -.
DR PDBsum; 2I5M; -.
DR PDBsum; 3PF4; -.
DR PDBsum; 3PF5; -.
DR PDBsum; 6SZZ; -.
DR PDBsum; 6T00; -.
DR AlphaFoldDB; P32081; -.
DR SMR; P32081; -.
DR STRING; 224308.BSU09100; -.
DR jPOST; P32081; -.
DR PaxDb; P32081; -.
DR PRIDE; P32081; -.
DR EnsemblBacteria; CAB12738; CAB12738; BSU_09100.
DR GeneID; 64302783; -.
DR GeneID; 936224; -.
DR KEGG; bsu:BSU09100; -.
DR PATRIC; fig|224308.179.peg.983; -.
DR eggNOG; COG1278; Bacteria.
DR InParanoid; P32081; -.
DR OMA; HYSTIKM; -.
DR PhylomeDB; P32081; -.
DR BioCyc; BSUB:BSU09100-MON; -.
DR EvolutionaryTrace; P32081; -.
DR PRO; PR:P32081; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0009295; C:nucleoid; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0001072; F:transcription antitermination factor activity, RNA binding; IBA:GO_Central.
DR GO; GO:0060567; P:negative regulation of DNA-templated transcription, termination; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR CDD; cd04458; CSP_CDS; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR012156; Cold_shock_CspA.
DR InterPro; IPR011129; CSD.
DR InterPro; IPR019844; CSD_1.
DR InterPro; IPR002059; CSP_DNA-bd.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR Pfam; PF00313; CSD; 1.
DR PIRSF; PIRSF002599; Cold_shock_A; 1.
DR PRINTS; PR00050; COLDSHOCK.
DR SMART; SM00357; CSP; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR PROSITE; PS00352; CSD_1; 1.
DR PROSITE; PS51857; CSD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Cytoplasm; Direct protein sequencing; DNA-binding;
KW Reference proteome; Stress response; Transcription;
KW Transcription regulation.
FT CHAIN 1..67
FT /note="Cold shock protein CspB"
FT /id="PRO_0000100295"
FT DOMAIN 4..63
FT /note="CSD"
FT VARIANT 17
FT /note="F -> L (in strain: Globigii)"
FT VARIANT 44
FT /note="G -> S (in strain: Globigii)"
FT VARIANT 46
FT /note="A -> S"
FT STRAND 2..10
FT /evidence="ECO:0007829|PDB:3PF4"
FT TURN 11..14
FT /evidence="ECO:0007829|PDB:3PF4"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:3PF4"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:6SZZ"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:3PF4"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:3PF4"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:3PF4"
FT STRAND 46..54
FT /evidence="ECO:0007829|PDB:3PF4"
FT STRAND 57..65
FT /evidence="ECO:0007829|PDB:3PF4"
SQ SEQUENCE 67 AA; 7365 MW; 1E7340FDB19E5BDC CRC64;
MLEGKVKWFN SEKGFGFIEV EGQDDVFVHF SAIQGEGFKT LEEGQAVSFE IVEGNRGPQA
ANVTKEA
