ID   A0A0A5I6X3_9BACI        Unreviewed;       210 AA.
AC   A0A0A5I6X3;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Photosynthetic protein synthase I {ECO:0000313|EMBL:KGX91577.1};
GN   ORFNames=N781_03545 {ECO:0000313|EMBL:KGX91577.1};
OS   Pontibacillus halophilus JSM 076056 = DSM 19796.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Pontibacillus.
OX   NCBI_TaxID=1385510 {ECO:0000313|EMBL:KGX91577.1, ECO:0000313|Proteomes:UP000030528};
RN   [1] {ECO:0000313|EMBL:KGX91577.1, ECO:0000313|Proteomes:UP000030528}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JSM 076056 {ECO:0000313|EMBL:KGX91577.1,
RC   ECO:0000313|Proteomes:UP000030528};
RA   Huang J., Wang G.;
RL   Submitted (AUG-2013) 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:KGX91577.1}.
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DR   EMBL; AVPE01000009; KGX91577.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A5I6X3; -.
DR   STRING; 1385510.GCA_000425205_02363; -.
DR   eggNOG; COG1999; Bacteria.
DR   Proteomes; UP000030528; 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; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030528};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..210
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038553085"
FT   DOMAIN          41..208
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   BINDING         79
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         83
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         171
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        79..83
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   210 AA;  23578 MW;  A07F10DD237C76F7 CRC64;
     MKKRMFTYTI VLIGVMILSA CGSQDSDSTS NSGGQAAMAE PEFSRDVRSF SFTNQDEETV
     SLEDLEGTYW IADMIFTNCD TVCPPMTANM AYLQDQVEEA GLSDEVRFVS FSVDPTVDSP
     SVLKDFAMKH EADFSNWDFL TGYSNEEIKE FSIKSFQLLV QHTDQSDQVT HGTNFMLVNP
     DGKAIERYKG MQRGEMERIV ADLESKIESS
//