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 02-SEP-2026, entry version 119. DE RecName: Full=Cold shock protein CspB; GN Name=cspB; OS Bacillus caldolyticus. OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Anoxybacillaceae; OC Geobacillus; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 AlphaFoldDB; P41016; -. DR SMR; P41016; -. DR GeneID; 94900531; -. DR EvolutionaryTrace; P41016; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0010468; P:regulation of gene expression; IEA:UniProtKB-ARBA. DR GO; GO:0051252; P:regulation of RNA metabolic process; IEA:UniProtKB-ARBA. DR CDD; cd04458; CSP_CDS; 1. DR FunFam; 2.40.50.140:FF:000006; Cold shock protein CspC; 1. DR Gene3D; 6.20.370.130; -; 1. DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1. DR InterPro; IPR012156; Cold_shock_CspA. DR InterPro; IPR050181; Cold_shock_domain. DR InterPro; IPR011129; CSD. DR InterPro; IPR019844; CSD_CS. DR InterPro; IPR002059; CSP_DNA-bd. DR InterPro; IPR012340; NA-bd_OB-fold. DR PANTHER; PTHR11544; COLD SHOCK DOMAIN CONTAINING PROTEINS; 1. DR Pfam; PF00313; CSD; 1. DR PIRSF; PIRSF002599; Cold_shock_A; 1. DR PRINTS; PR00050; COLDSHOCK. DR SMART; SM00357; CSP; 1. DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1. DR PROSITE; PS00352; CSD_1; 1. DR PROSITE; PS51857; CSD_2; 1. DR PDBsum; 1C9O; -. DR PDBsum; 1HZ9; -. DR PDBsum; 1HZA; -. DR PDBsum; 1HZB; -. DR PDBsum; 1HZC; -. DR PDBsum; 1I5F; -. DR PDBsum; 2HAX; -. DR PDBsum; 5JX4; -. 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 //