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Database: UniProt
Entry: A0A0M0GF44_SPOGL
LinkDB: A0A0M0GF44_SPOGL
Original site: A0A0M0GF44_SPOGL 
ID   A0A0M0GF44_SPOGL        Unreviewed;       199 AA.
AC   A0A0M0GF44;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Manganese transporter {ECO:0000313|EMBL:KON88459.1};
GN   ORFNames=AF332_17670 {ECO:0000313|EMBL:KON88459.1};
OS   Sporosarcina globispora (Bacillus globisporus).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Sporosarcina.
OX   NCBI_TaxID=1459 {ECO:0000313|EMBL:KON88459.1, ECO:0000313|Proteomes:UP000037109};
RN   [1] {ECO:0000313|Proteomes:UP000037109}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4 {ECO:0000313|Proteomes:UP000037109};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA   Shi H., Pan Z., Liu X.;
RT   "Fjat-10036 dsm4.";
RL   Submitted (JUL-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:KON88459.1}.
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DR   EMBL; LGUF01000007; KON88459.1; -; Genomic_DNA.
DR   RefSeq; WP_053435833.1; NZ_LGUF01000007.1.
DR   AlphaFoldDB; A0A0M0GF44; -.
DR   STRING; 1459.AF332_17670; -.
DR   PATRIC; fig|1459.3.peg.3874; -.
DR   OrthoDB; 9811998at2; -.
DR   Proteomes; UP000037109; 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   InterPro; IPR013766; Thioredoxin_domain.
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; 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   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR603782-1}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          26..199
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   BINDING         65
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         69
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         163
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        65..69
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   199 AA;  23208 MW;  6A6482286257DEC5 CRC64;
     MKKVYIISAI IVVLGITAGI SFFIFRDMTA KIPDHITLLT DDEKVYDFAE SDKKLKLVEF
     IYTHCPDICP TTTQRMNMLK GDLSKEGVFG EKVQFVTVTI DPYRDTADVL RKYRDTFEIE
     NDENWVFLTA DPDNLKKDQA EIQELANTFQ FQYRDPGDGF YVHSTFVYLL DENNKFIKKF
     PMGEDFDKND VFSKIMKEI
//
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