ID Q9K3L0_STRCO Unreviewed; 200 AA. AC Q9K3L0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 09-DEC-2015, entry version 85. DE SubName: Full=Putative DNA protection protein {ECO:0000313|EMBL:CAB96035.1}; GN OrderedLocusNames=SCO1050 {ECO:0000313|EMBL:CAB96035.1}; OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145). OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces; Streptomyces albidoflavus group. OX NCBI_TaxID=100226 {ECO:0000313|Proteomes:UP000001973}; RN [1] {ECO:0000213|PDB:4CYB} RP X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) OF 28-200 IN COMPLEX WITH IRON. RX PubMed=24915944; DOI=10.1007/S00018-014-1658-4; RA Hitchings M.D., Townsend P., Pohl E., Facey P.D., Jones D.H., RA Dyson P.J., Del Sol R.; RT "A tale of tails: deciphering the contribution of terminal tails to RT the biochemical properties of two Dps proteins from Streptomyces RT coelicolor."; RL Cell. Mol. Life Sci. 71:4911-4926(2014). CC -!- SIMILARITY: Belongs to the Dps family. CC {ECO:0000256|RuleBase:RU003875}. 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; AL939107; CAB96035.1; -; Genomic_DNA. DR RefSeq; NP_625345.1; NC_003888.3. DR RefSeq; WP_003977779.1; NC_003888.3. DR PDB; 4CYB; X-ray; 1.78 A; A/B/C/D/E/F/G/H/I/J/K/L=28-200. DR PDBsum; 4CYB; -. DR ProteinModelPortal; Q9K3L0; -. DR STRING; 100226.SCO1050; -. DR EnsemblBacteria; CAB96035; CAB96035; CAB96035. DR GeneID; 1096473; -. DR KEGG; sco:SCO1050; -. DR PATRIC; 23731646; VBIStrCoe124346_1045. DR eggNOG; COG0783; LUCA. DR eggNOG; ENOG4107V21; Bacteria. DR HOGENOM; HOG000273542; -. DR InParanoid; Q9K3L0; -. DR KO; K04047; -. DR OMA; QVWFLSE; -. DR OrthoDB; EOG6Z9B6G; -. DR PhylomeDB; Q9K3L0; -. DR Proteomes; UP000001973; Chromosome. DR GO; GO:0005623; C:cell; IEA:GOC. DR GO; GO:0008199; F:ferric iron binding; IEA:InterPro. DR GO; GO:0016722; F:oxidoreductase activity, oxidizing metal ions; IEA:InterPro. DR GO; GO:0006879; P:cellular iron ion homeostasis; IEA:InterPro. DR GO; GO:0006950; P:response to stress; IEA:InterPro. DR Gene3D; 1.20.1260.10; -; 1. DR InterPro; IPR002177; DPS_DNA-bd. DR InterPro; IPR023188; DPS_DNA-bd_CS. DR InterPro; IPR009078; Ferritin-like_SF. DR InterPro; IPR012347; Ferritin-rel. DR InterPro; IPR008331; Ferritin_DPS_dom. DR Pfam; PF00210; Ferritin; 1. DR PIRSF; PIRSF005900; Dps; 1. DR PRINTS; PR01346; HELNAPAPROT. DR SUPFAM; SSF47240; SSF47240; 1. DR PROSITE; PS00818; DPS_1; 1. DR PROSITE; PS00819; DPS_2; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:4CYB}; KW Complete proteome {ECO:0000313|Proteomes:UP000001973}; KW Iron {ECO:0000213|PDB:4CYB}; Metal-binding {ECO:0000213|PDB:4CYB}; KW Reference proteome {ECO:0000313|Proteomes:UP000001973}. FT DOMAIN 53 196 Ferritin. {ECO:0000259|Pfam:PF00210}. FT METAL 73 73 Iron; via tele nitrogen. FT {ECO:0000213|PDB:4CYB}. FT METAL 100 100 Iron. {ECO:0000213|PDB:4CYB}. FT METAL 104 104 Iron. {ECO:0000213|PDB:4CYB}. SQ SEQUENCE 200 AA; 22518 MW; 78863EA01B6ECF80 CRC64; MSSPKPKPPS SAEHRSDGSQ PWLHQKGRTI QEFGTVKQFP VALTMDTRLY SCQRLNKVLA DTRILHDLYK KYHWLMRGAT FYQLHLLLDK HAGEQLELID TVAERVQTLG GVAVGDPRHV AEITTVPRPP DGVEEVPSML SRLLEAHELI LTECHDAAAR TQEYGDDGTN DLLVSEVLRT NELQAWFVAE HLVDTPLVHA //