ID   GRIE_STRGG              Reviewed;         129 AA.
AC   B1VTI4; Q4W5X2;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   25-MAY-2022, entry version 46.
DE   RecName: Full=Copper chaperone GriE;
DE   AltName: Full=Grixazone biosynthesis protein E;
DE   Flags: Precursor;
GN   Name=griE; OrderedLocusNames=SGR_4245;
OS   Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=455632;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=JCM 4626 / NBRC 13350;
RX   PubMed=16282322; DOI=10.1074/jbc.m505806200;
RA   Suzuki H., Furusho Y., Higashi T., Ohnishi Y., Horinouchi S.;
RT   "A novel o-aminophenol oxidase responsible for formation of the
RT   phenoxazinone chromophore of grixazone.";
RL   J. Biol. Chem. 281:824-833(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 4626 / NBRC 13350;
RX   PubMed=18375553; DOI=10.1128/jb.00204-08;
RA   Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA   Yamashita A., Hattori M., Horinouchi S.;
RT   "Genome sequence of the streptomycin-producing microorganism Streptomyces
RT   griseus IFO 13350.";
RL   J. Bacteriol. 190:4050-4060(2008).
CC   -!- FUNCTION: Involved in the transfer of copper ion to the apo form O-
CC       aminophenol oxidase GriF in the grixazone biosynthetic pathway.
CC       {ECO:0000305|PubMed:16282322}.
CC   -!- PTM: Predicted to be exported by the Tat system. The position of the
CC       signal peptide cleavage has not been experimentally proven.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking griE and griF show accumulation of
CC       the 3-amino-4-hydroxybenzaldehyde (3,4-AHBAL) intermediate.
CC       {ECO:0000269|PubMed:16282322}.
CC   -!- SIMILARITY: Belongs to the melC1 family. {ECO:0000305}.
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DR   EMBL; AB214954; BAD99128.1; -; Genomic_DNA.
DR   EMBL; AB259663; BAF36647.1; -; Genomic_DNA.
DR   EMBL; AP009493; BAG21074.1; -; Genomic_DNA.
DR   RefSeq; WP_012380458.1; NC_010572.1.
DR   AlphaFoldDB; B1VTI4; -.
DR   SMR; B1VTI4; -.
DR   STRING; 455632.SGR_4245; -.
DR   EnsemblBacteria; BAG21074; BAG21074; SGR_4245.
DR   GeneID; 6210973; -.
DR   KEGG; sgr:SGR_4245; -.
DR   PATRIC; fig|455632.4.peg.4325; -.
DR   eggNOG; ENOG502ZWEF; Bacteria.
DR   HOGENOM; CLU_130429_1_0_11; -.
DR   OrthoDB; 2054156at2; -.
DR   Proteomes; UP000001685; Chromosome.
DR   GO; GO:0005507; F:copper ion binding; TAS:UniProtKB.
DR   GO; GO:0042438; P:melanin biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.30.1880.10; -; 1.
DR   InterPro; IPR023199; GriE/MELC1_sf.
DR   InterPro; IPR010928; MelC1.
DR   InterPro; IPR006311; TAT_signal.
DR   Pfam; PF06236; MelC1; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Copper; Signal.
FT   SIGNAL          1..37
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT   CHAIN           38..129
FT                   /note="Copper chaperone GriE"
FT                   /id="PRO_0000418467"
FT   REGION          32..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   129 AA;  13427 MW;  BEF901E3223F4CD8 CRC64;
     MPMNRREMVM ATTGAALAAA AAVPLLSGGE GEGAAEAAAA PAKATGRGRE HTERYLGRSI
     RVAAPADGGG VFIDGRPLHI MKFADDAYLS SMCHYEMAPT PLHAARRAVE ELRGAALQPS
     THGTHVTHL