ID H2CE84_9LEPT Unreviewed; 188 AA.
AC H2CE84;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Electron transport protein SCO1/SenC {ECO:0000313|EMBL:EHQ07639.1};
GN ORFNames=Lepil_2974 {ECO:0000313|EMBL:EHQ07639.1};
OS Leptonema illini DSM 21528.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptonema.
OX NCBI_TaxID=929563 {ECO:0000313|EMBL:EHQ07639.1, ECO:0000313|Proteomes:UP000005737};
RN [1] {ECO:0000313|EMBL:EHQ07639.1, ECO:0000313|Proteomes:UP000005737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21528 {ECO:0000313|EMBL:EHQ07639.1,
RC ECO:0000313|Proteomes:UP000005737};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Held B.,
RA Kyrpides N., Mavromatis K., Ivanova N., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S., Brambilla E.-M.,
RA Klenk H.-P., Eisen J.A.;
RT "The Improved High-Quality Draft genome of Leptonema illini DSM 21528.";
RL Submitted (OCT-2011) 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; JH597773; EHQ07639.1; -; Genomic_DNA.
DR RefSeq; WP_002773676.1; NZ_JH597773.1.
DR AlphaFoldDB; H2CE84; -.
DR STRING; 183.GCA_002009735_04118; -.
DR HOGENOM; CLU_050131_3_1_12; -.
DR Proteomes; UP000005737; 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: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.
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:UP000005737};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..188
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003559711"
FT BINDING 64
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 68
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 153
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT DISULFID 64..68
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ SEQUENCE 188 AA; 20815 MW; 8225BB06BEA1444C CRC64;
MVRSRLIILI SLAMLSFTAC KKETAPQRSV HSWNMTSLVD ETGAAVALKS IERPKVVFFG
YSHCPDMCPA ALSQLAKAVK ILGRDGNRIT PVFISLDPSR DTPETLSAYR DQFDERKLRA
FTGDRDQIDR LAKDFGVMYK QSENAAVGYG IDHTGFYYLL NDGDGLLLAL PVGLSAVELA
EQLRETLL
//
