ID A0A0F3NPD5_9RICK Unreviewed; 219 AA.
AC A0A0F3NPD5;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=AhpC/TSA family protein {ECO:0000313|EMBL:KJV69547.1};
GN ORFNames=NLO413_0940 {ECO:0000313|EMBL:KJV69547.1};
OS Candidatus Neoehrlichia lotoris str. RAC413.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Neoehrlichia.
OX NCBI_TaxID=1359163 {ECO:0000313|EMBL:KJV69547.1, ECO:0000313|Proteomes:UP000033562};
RN [1] {ECO:0000313|EMBL:KJV69547.1, ECO:0000313|Proteomes:UP000033562}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RAC413 {ECO:0000313|EMBL:KJV69547.1,
RC ECO:0000313|Proteomes:UP000033562};
RA Daugherty S.C., Su Q., Abolude K., Beier-Sexton M., Carlyon J.A.,
RA Carter R., Day N.P., Dumler S.J., Dyachenko V., Godinez A., Kurtti T.J.,
RA Lichay M., Mullins K.E., Ott S., Pappas-Brown V., Paris D.H., Patel P.,
RA Richards A.L., Sadzewicz L., Sears K., Seidman D., Sengamalay N.,
RA Stenos J., Tallon L.J., Vincent G., Fraser C.M., Munderloh U.,
RA Dunning-Hotopp J.C.;
RT "Genome Sequencing of Rickettsiales.";
RL Submitted (FEB-2015) 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:KJV69547.1}.
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DR EMBL; LANX01000001; KJV69547.1; -; Genomic_DNA.
DR RefSeq; WP_045809230.1; NZ_LANX01000001.1.
DR AlphaFoldDB; A0A0F3NPD5; -.
DR STRING; 1359163.NLO413_0940; -.
DR PATRIC; fig|1359163.3.peg.913; -.
DR OrthoDB; 9790194at2; -.
DR Proteomes; UP000033562; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|PIRSR:PIRSR603782-1};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR603782-2};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR603782-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000033562};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 83
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 87
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 168
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT DISULFID 83..87
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ SEQUENCE 219 AA; 24846 MW; E49F4F563115AC06 CRC64;
MKIFKILSNT FLLLAAMFLV YSYFNKKGIF NKGNSHNVNV LNIKNNQGSF DTSFNLINQE
GVNVSSKDFA GKYMLVIFGF SSCNHICPAE LGLASELLSK LENNADKIQV IFITIDPERD
TVERLKEYHQ GFDNRIQMLT GSKQDLDKVA KNYKVYVGGQ DSDKQIDHSS LLYLIDQNGN
FLTHFAPDLK SSKNQTEKLF LLVKQYLTPQ EPNNQNTVS
//
