ID DBPB_BORBU Reviewed; 187 AA. AC P0CL68; O50918; O52611; DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot. DT 05-APR-2011, sequence version 1. DT 27-MAR-2024, entry version 43. DE RecName: Full=Decorin-binding protein B; DE Flags: Precursor; GN Name=dbpB; OrderedLocusNames=BB_A25; OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) OS (Borrelia burgdorferi). OG Plasmid lp54. OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Borreliaceae; OC Borreliella. OX NCBI_TaxID=224326; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31; RX PubMed=9403685; DOI=10.1038/37551; RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A., RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L., RA Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L., RA Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M., RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F., RA Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C., RA Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B., RA Smith H.O., Venter J.C.; RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi."; RL Nature 390:580-586(1997). CC -!- FUNCTION: Binds to decorin which may mediate the adherence of CC B.burgdorferi to collagen fibers in skin and other tissues. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the decorin-binding protein family. CC {ECO:0000305}. 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; AE000790; AAC66244.1; -; Genomic_DNA. DR PIR; A70210; A70210. DR RefSeq; NP_045698.1; NC_001857.2. DR RefSeq; WP_010890381.1; NC_001857.2. DR PDB; 2MVG; NMR; -; A=22-187. DR PDBsum; 2MVG; -. DR AlphaFoldDB; P0CL68; -. DR BMRB; P0CL68; -. DR SMR; P0CL68; -. DR EnsemblBacteria; AAC66244; AAC66244; BB_A25. DR KEGG; bbu:BB_A25; -. DR PATRIC; fig|224326.49.peg.1542; -. DR HOGENOM; CLU_124841_0_0_12; -. DR OrthoDB; 352280at2; -. DR Proteomes; UP000001807; Plasmid lp54. DR Gene3D; 1.20.1420.40; Decorin-binding protein; 1. DR InterPro; IPR003332; Decorin-bd. DR InterPro; IPR038353; Decorin-db_sf. DR NCBIfam; NF033720; DbpB; 1. DR Pfam; PF02352; Decorin_bind; 1. PE 1: Evidence at protein level; KW 3D-structure; Plasmid; Reference proteome; Signal. FT SIGNAL 1..20 FT /evidence="ECO:0000255" FT CHAIN 21..187 FT /note="Decorin-binding protein B" FT /id="PRO_0000021075" FT TURN 27..31 FT /evidence="ECO:0007829|PDB:2MVG" FT HELIX 34..53 FT /evidence="ECO:0007829|PDB:2MVG" FT TURN 70..74 FT /evidence="ECO:0007829|PDB:2MVG" FT HELIX 75..102 FT /evidence="ECO:0007829|PDB:2MVG" FT TURN 103..105 FT /evidence="ECO:0007829|PDB:2MVG" FT HELIX 108..120 FT /evidence="ECO:0007829|PDB:2MVG" FT TURN 121..123 FT /evidence="ECO:0007829|PDB:2MVG" FT HELIX 124..128 FT /evidence="ECO:0007829|PDB:2MVG" FT HELIX 134..143 FT /evidence="ECO:0007829|PDB:2MVG" FT HELIX 150..167 FT /evidence="ECO:0007829|PDB:2MVG" FT HELIX 168..171 FT /evidence="ECO:0007829|PDB:2MVG" FT STRAND 174..178 FT /evidence="ECO:0007829|PDB:2MVG" SQ SEQUENCE 187 AA; 20398 MW; 7AC8CCF8C690E526 CRC64; MKIGKLNSIV IALFFKLLVA CSIGLVERTN AALESSSKDL KNKILKIKKE ATGKGVLFEA FTGLKTGSKV TSGGLALREA KVQAIVETGK FLKIIEEEAL KLKETGNSGQ FLAMFDLMLE VVESLEDVGI IGLKARVLEE SKNNPINTAE RLLAAKAQIE NQLKVVKEKQ NIENGGEKKN NKSKKKK //