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Database: UniProt
Entry: S5TXI7_9GAMM
LinkDB: S5TXI7_9GAMM
Original site: S5TXI7_9GAMM 
ID   S5TXI7_9GAMM            Unreviewed;       193 AA.
AC   S5TXI7;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Cytochrome oxidase biogenesis protein Sco1/SenC/PrrC, putative copper metallochaperone {ECO:0000313|EMBL:AGS39865.1};
GN   ORFNames=CYCME_1540 {ECO:0000313|EMBL:AGS39865.1};
OS   Cycloclasticus zancles 78-ME.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Cycloclasticus.
OX   NCBI_TaxID=1198232 {ECO:0000313|EMBL:AGS39865.1, ECO:0000313|Proteomes:UP000015380};
RN   [1] {ECO:0000313|EMBL:AGS39865.1, ECO:0000313|Proteomes:UP000015380}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=7-ME {ECO:0000313|Proteomes:UP000015380};
RA   Yakimov M.M., Messina E., Genovese M., Denaro R., Crisafi F., Russo D.,
RA   Cappello S., Santisi S., Smedile F., Golyshina O.V., Tran H., Pieper D.H.,
RA   Golyshin P.N., Giuliano L.;
RT   "Between feast and famine: a lifestyle of most important marine PAH-
RT   degrading bacterium Cycloclasticus sp. 7ME.";
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the SCO1/2 family.
CC       {ECO:0000256|ARBA:ARBA00010996}.
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DR   EMBL; CP005996; AGS39865.1; -; Genomic_DNA.
DR   AlphaFoldDB; S5TXI7; -.
DR   KEGG; cza:CYCME_1540; -.
DR   PATRIC; fig|1198232.3.peg.1525; -.
DR   eggNOG; COG1999; Bacteria.
DR   HOGENOM; CLU_050131_3_0_6; -.
DR   Proteomes; UP000015380; Chromosome.
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; ELECTRON TRANSPORT PROTIN SCO1/SENC FAMILY MEMBER; 1.
DR   PANTHER; PTHR12151:SF25; SCO1 PROTEIN HOMOLOG; 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}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..193
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004541052"
FT   DOMAIN          28..192
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   BINDING         68
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         72
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         157
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        68..72
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   193 AA;  21096 MW;  E135CEEC4489A039 CRC64;
     MKKIKSIAAI AILITLSACA EDEPTRLTNV SGLIPDLSFE LIDEDNKVVT ASDYHGYTVA
     LFFGFTNCPG ICPTTMHQLS QVLADVDPEG SSMKVLFVSV DPKRDTVEKL KKYTDIFGPA
     FIGLRGDESA VKEMTKKYRV TFGYGDSDAQ GNYEVSHSGA VFVFDSKGEA KLLATQSSTT
     EDMIYDVKKL VNL
//
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