ID G2G6W5_9ACTN Unreviewed; 219 AA.
AC G2G6W5;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Secreted protein {ECO:0000313|EMBL:EGX60678.1};
GN ORFNames=SZN_06114 {ECO:0000313|EMBL:EGX60678.1};
OS Streptomyces zinciresistens K42.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=700597 {ECO:0000313|EMBL:EGX60678.1, ECO:0000313|Proteomes:UP000004217};
RN [1] {ECO:0000313|EMBL:EGX60678.1, ECO:0000313|Proteomes:UP000004217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K42 {ECO:0000313|EMBL:EGX60678.1,
RC ECO:0000313|Proteomes:UP000004217};
RA Lin Y., Hao X., Johnstone L., Miller S.J., Wei G., Rensing C.;
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the SCO1/2 family.
CC {ECO:0000256|ARBA:ARBA00010996}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGX60678.1}.
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DR EMBL; AGBF01000011; EGX60678.1; -; Genomic_DNA.
DR RefSeq; WP_007492418.1; NZ_AGBF01000011.1.
DR AlphaFoldDB; G2G6W5; -.
DR PATRIC; fig|700597.3.peg.1181; -.
DR OrthoDB; 9790194at2; -.
DR Proteomes; UP000004217; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd02968; SCO; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR003782; SCO1/SenC.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR12151:SF5; AT19154P; 1.
DR PANTHER; PTHR12151; ELECTRON TRANSPORT PROTIN SCO1/SENC FAMILY MEMBER; 1.
DR Pfam; PF02630; SCO1-SenC; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|PIRSR:PIRSR603782-1};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR603782-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR603782-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000004217};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..219
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038519663"
FT DOMAIN 50..212
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT BINDING 89
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 93
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 179
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT DISULFID 89..93
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ SEQUENCE 219 AA; 23250 MW; 8A79CE0EA9562FA6 CRC64;
MRKQALATAA LLAVAALTLT ACGGGADSSD KPPVTVVSEQ PGSDKAAIVL DTPFEKPDLV
LTDTNGKKYD FRKETAGKAT LVYFGYTSCP DVCPTTMSNI AVAKKQLPKD QQDALRVVFI
TTDPVRDTSA ALGKWLKGID PQIVGLTGAF PTVQAAARTV GITIEPPYKD KNGRMVSTHG
TQVIAFSPKS DDGYVVYTED TLVDDYAKDL PKLLKGAKP
//
