BLE_STRHI
ID BLE_STRHI Reviewed; 124 AA.
AC P17493;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Bleomycin resistance protein;
DE Short=BRP;
DE AltName: Full=Phleomycin resistance protein;
GN Name=ble;
OS Streptoalloteichus hindustanus.
OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC Streptoalloteichus.
OX NCBI_TaxID=2017;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 31158 / E465-94;
RX PubMed=1695734; DOI=10.1093/nar/18.13.4009;
RA Drocourt D., Calmels T., Reynes J.-P., Baron M., Tiraby G.;
RT "Cassettes of the Streptoalloteichus hindustanus ble gene for
RT transformation of lower and higher eukaryotes to phleomycin resistance.";
RL Nucleic Acids Res. 18:4009-4009(1990).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RC STRAIN=ATCC 31158 / E465-94;
RX PubMed=7516875; DOI=10.1002/j.1460-2075.1994.tb06535.x;
RA Dumas P., Bergdoll M., Cagnon C., Masson J.-M.;
RT "Crystal structure and site-directed mutagenesis of a bleomycin resistance
RT protein and their significance for drug sequestering.";
RL EMBO J. 13:2483-2492(1994).
CC -!- FUNCTION: Binding protein with a strong affinity to the bleomycin
CC family of antibiotics.
CC -!- SUBUNIT: Homodimer.
CC -!- SIMILARITY: Belongs to the bleomycin resistance protein family.
CC {ECO:0000305}.
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DR EMBL; X52869; CAA37050.1; -; Genomic_DNA.
DR PIR; S10304; S10304.
DR RefSeq; WP_063842998.1; NZ_FQVN01000005.1.
DR PDB; 1BYL; X-ray; 2.30 A; A=1-124.
DR PDB; 1XRK; X-ray; 1.50 A; A/B=1-124.
DR PDB; 2ZHP; X-ray; 1.60 A; A/B=1-124.
DR PDBsum; 1BYL; -.
DR PDBsum; 1XRK; -.
DR PDBsum; 2ZHP; -.
DR AlphaFoldDB; P17493; -.
DR BMRB; P17493; -.
DR SMR; P17493; -.
DR EvolutionaryTrace; P17493; -.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR CDD; cd08349; BLMA_like; 1.
DR Gene3D; 3.10.180.10; -; 1.
DR InterPro; IPR000335; Bleomycin-R.
DR InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
DR InterPro; IPR037523; VOC.
DR Pfam; PF19581; Glyoxalase_7; 1.
DR PRINTS; PR00311; BLEOMYCINRST.
DR SUPFAM; SSF54593; SSF54593; 1.
DR PROSITE; PS51819; VOC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance.
FT CHAIN 1..124
FT /note="Bleomycin resistance protein"
FT /id="PRO_0000068563"
FT DOMAIN 3..121
FT /note="VOC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT STRAND 3..14
FT /evidence="ECO:0007829|PDB:1XRK"
FT HELIX 16..25
FT /evidence="ECO:0007829|PDB:1XRK"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:1XRK"
FT STRAND 36..43
FT /evidence="ECO:0007829|PDB:1XRK"
FT STRAND 46..52
FT /evidence="ECO:0007829|PDB:1XRK"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:1XRK"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:1XRK"
FT STRAND 63..69
FT /evidence="ECO:0007829|PDB:1XRK"
FT HELIX 71..78
FT /evidence="ECO:0007829|PDB:1XRK"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:1XRK"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:1XRK"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:1XRK"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:1BYL"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:1XRK"
FT STRAND 103..109
FT /evidence="ECO:0007829|PDB:1XRK"
FT STRAND 115..120
FT /evidence="ECO:0007829|PDB:1XRK"
SQ SEQUENCE 124 AA; 13796 MW; 13CCB17F1CC14887 CRC64;
MAKLTSAVPV LTARDVAGAV EFWTDRLGFS RDFVEDDFAG VVRDDVTLFI SAVQDQVVPD
NTLAWVWVRG LDELYAEWSE VVSTNFRDAS GPAMTEIGEQ PWGREFALRD PAGNCVHFVA
EEQD