ID   CSPB_BACCL              Reviewed;          66 AA.
AC   P41016;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=Cold shock protein CspB;
GN   Name=cspB;
OS   Bacillus caldolyticus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   Geobacillus thermoleovorans group.
OX   NCBI_TaxID=1394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.17 ANGSTROMS).
RX   PubMed=10736231; DOI=10.1006/jmbi.2000.3602;
RA   Mueller U., Perl D., Schmid F.X., Heinemann U.;
RT   "Thermal stability and atomic-resolution crystal structure of the Bacillus
RT   caldolyticus cold shock protein.";
RL   J. Mol. Biol. 297:975-988(2000).
CC   -!- FUNCTION: Affects cell viability at low temperatures.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- INDUCTION: In response to low temperature. {ECO:0000250}.
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DR   EMBL; X73373; CAA51790.1; -; Genomic_DNA.
DR   PIR; I40158; I40158.
DR   RefSeq; WP_003251474.1; NZ_CP025074.1.
DR   PDB; 1C9O; X-ray; 1.17 A; A/B=1-66.
DR   PDB; 1HZ9; X-ray; 1.80 A; A/B=1-66.
DR   PDB; 1HZA; X-ray; 1.80 A; A/B=1-66.
DR   PDB; 1HZB; X-ray; 1.28 A; A/B=1-66.
DR   PDB; 1HZC; X-ray; 1.32 A; A/B=1-66.
DR   PDB; 1I5F; X-ray; 1.40 A; A/B=1-66.
DR   PDB; 2HAX; X-ray; 1.29 A; A/B=1-66.
DR   PDB; 5JX4; X-ray; 1.80 A; A/B=1-66.
DR   PDBsum; 1C9O; -.
DR   PDBsum; 1HZ9; -.
DR   PDBsum; 1HZA; -.
DR   PDBsum; 1HZB; -.
DR   PDBsum; 1HZC; -.
DR   PDBsum; 1I5F; -.
DR   PDBsum; 2HAX; -.
DR   PDBsum; 5JX4; -.
DR   AlphaFoldDB; P41016; -.
DR   SMR; P41016; -.
DR   GeneID; 56925764; -.
DR   EvolutionaryTrace; P41016; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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; DNA-binding; Stress response;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..66
FT                   /note="Cold shock protein CspB"
FT                   /id="PRO_0000100280"
FT   DOMAIN          4..63
FT                   /note="CSD"
FT   STRAND          2..10
FT                   /evidence="ECO:0007829|PDB:1C9O"
FT   TURN            11..14
FT                   /evidence="ECO:0007829|PDB:1C9O"
FT   STRAND          15..20
FT                   /evidence="ECO:0007829|PDB:1C9O"
FT   STRAND          23..29
FT                   /evidence="ECO:0007829|PDB:1C9O"
FT   HELIX           30..32
FT                   /evidence="ECO:0007829|PDB:1C9O"
FT   STRAND          35..37
FT                   /evidence="ECO:0007829|PDB:1C9O"
FT   STRAND          46..54
FT                   /evidence="ECO:0007829|PDB:1C9O"
FT   STRAND          57..65
FT                   /evidence="ECO:0007829|PDB:1C9O"
SQ   SEQUENCE   66 AA;  7333 MW;  0C811F714B0BC784 CRC64;
     MQRGKVKWFN NEKGYGFIEV EGGSDVFVHF TAIQGEGFKT LEEGQEVSFE IVQGNRGPQA
     ANVVKL