ID A0A1E5CVQ5_9VIBR Unreviewed; 206 AA.
AC A0A1E5CVQ5;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Photosynthetic protein synthase I {ECO:0000313|EMBL:OEE73642.1};
GN ORFNames=A130_06910 {ECO:0000313|EMBL:OEE73642.1};
OS Vibrio genomosp. F6 str. FF-238.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1191298 {ECO:0000313|EMBL:OEE73642.1, ECO:0000313|Proteomes:UP000094165};
RN [1] {ECO:0000313|EMBL:OEE73642.1, ECO:0000313|Proteomes:UP000094165}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FF-238 {ECO:0000313|EMBL:OEE73642.1,
RC ECO:0000313|Proteomes:UP000094165};
RX PubMed=22955834; DOI=10.1126/science.1219385;
RA Cordero O.X., Wildschutte H., Kirkup B., Proehl S., Ngo L., Hussain F.,
RA Le Roux F., Mincer T., Polz M.F.;
RT "Ecological populations of bacteria act as socially cohesive units of
RT antibiotic production and resistance.";
RL Science 337:1228-1231(2012).
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:OEE73642.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJYW02000228; OEE73642.1; -; Genomic_DNA.
DR RefSeq; WP_017052242.1; NZ_AJYW02000228.1.
DR AlphaFoldDB; A0A1E5CVQ5; -.
DR Proteomes; UP000094165; 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 PANTHER; PTHR12151; ELECTRON TRANSPORT PROTIN SCO1/SENC FAMILY MEMBER; 1.
DR PANTHER; PTHR12151:SF27; PUTATIVE-RELATED; 1.
DR Pfam; PF02630; SCO1-SenC; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|PIRSR:PIRSR603782-1};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR603782-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR603782-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000094165}.
FT BINDING 75
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 79
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 166
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT DISULFID 75..79
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ SEQUENCE 206 AA; 22988 MW; 64E1BB278CEEBDA5 CRC64;
MSRNWSLILV VAFALGYGVK AYLDGQASIR LEQQQAAAEQ QAVNTVLFGK DNQEVAIFDP
QDPRIRIVYF GFTRCPDVCP TSLAMLSGAL NEIDPQQQSQ LRPIFISLDP ERDAADDSFK
YAQYFHPMIE GLSAPLEITT TLAHHYGVIF RKTELEGSQL EYTLDHSSYF YFLKPDGTLI
KKVPHTLSPA PIVEAINTLT QTSSEG
//
