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Database: UniProt
Entry: A0A125BD23_THIDE
LinkDB: A0A125BD23_THIDE
Original site: A0A125BD23_THIDE 
ID   A0A125BD23_THIDE        Unreviewed;       432 AA.
AC   A0A125BD23;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Magnesium and cobalt efflux protein CorC {ECO:0000313|EMBL:KVW97322.1};
GN   ORFNames=ABW22_04270 {ECO:0000313|EMBL:KVW97322.1};
OS   Thiobacillus denitrificans.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Thiobacillaceae; Thiobacillus.
OX   NCBI_TaxID=36861 {ECO:0000313|EMBL:KVW97322.1, ECO:0000313|Proteomes:UP000064243};
RN   [1] {ECO:0000313|EMBL:KVW97322.1, ECO:0000313|Proteomes:UP000064243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RG {ECO:0000313|EMBL:KVW97322.1,
RC   ECO:0000313|Proteomes:UP000064243};
RX   PubMed=26712544;
RA   Harrold Z.R., Skidmore M.L., Hamilton T.L., Desch L., Amada K.,
RA   van Gelder W., Glover K., Roden E.E., Boyd E.S.;
RT   "Aerobic and Anaerobic Thiosulfate Oxidation by a Cold-Adapted, Subglacial
RT   Chemoautotroph.";
RL   Appl. Environ. Microbiol. 82:1486-1495(2015).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:KVW97322.1}.
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DR   EMBL; LDUG01000016; KVW97322.1; -; Genomic_DNA.
DR   RefSeq; WP_059752259.1; NZ_LDUG01000016.1.
DR   AlphaFoldDB; A0A125BD23; -.
DR   STRING; 1123392.GCA_000376425_01996; -.
DR   PATRIC; fig|36861.3.peg.307; -.
DR   OrthoDB; 9797674at2; -.
DR   Proteomes; UP000064243; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   CDD; cd04590; CBS_pair_CorC_HlyC_assoc; 1.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.10.580.10; CBS-domain; 1.
DR   InterPro; IPR000644; CBS_dom.
DR   InterPro; IPR046342; CBS_dom_sf.
DR   InterPro; IPR002550; CNNM.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR044751; Ion_transp-like_CBS.
DR   InterPro; IPR005170; Transptr-assoc_dom.
DR   PANTHER; PTHR22777; HEMOLYSIN-RELATED; 1.
DR   PANTHER; PTHR22777:SF32; UPF0053 INNER MEMBRANE PROTEIN YFJD; 1.
DR   Pfam; PF00571; CBS; 2.
DR   Pfam; PF01595; CNNM; 1.
DR   Pfam; PF03471; CorC_HlyC; 1.
DR   SMART; SM01091; CorC_HlyC; 1.
DR   SUPFAM; SSF54631; CBS-domain pair; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   PROSITE; PS51371; CBS; 2.
DR   PROSITE; PS51846; CNNM; 1.
PE   4: Predicted;
KW   CBS domain {ECO:0000256|ARBA:ARBA00023122, ECO:0000256|PROSITE-
KW   ProRule:PRU00703};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW   ProRule:PRU01193}; Reference proteome {ECO:0000313|Proteomes:UP000064243};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW   ProRule:PRU01193};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|PROSITE-
KW   ProRule:PRU01193}.
FT   TRANSMEM        62..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        93..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        130..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          2..194
FT                   /note="CNNM transmembrane"
FT                   /evidence="ECO:0000259|PROSITE:PS51846"
FT   DOMAIN          211..271
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   DOMAIN          277..333
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
SQ   SEQUENCE   432 AA;  47544 MW;  1BFA6CF811CAD4C6 CRC64;
     MEALSISTLF GLLAGLLFLS AFFSASETAM MAINRYRLRH AAESGVRGAM RAQALLNQTD
     KLLGVILLGN NLVNIAAATL ATIISIRLFG DSDLALSLAT LLLTFLILVF SEVTPKVLGA
     SFPERVAYPA TLLLTPMLKL AYPVVWFVNL FVQGILRLLR IKPPEPGHGS RLGLEELRTI
     VLESSGLLPR EHHRILVNLL ELEDITVDDV MTPRNQIEAI DIEDDPERLR QQISTSHHTR
     LVVHAGSSDN LLGVLHVRRV LHALTGEELD PQTLKENLED PYFVPAGTPL FTQLRNFKNS
     RRRLALVVDE YGELQGLVTL EDLLEEMVGE FTTQAPSDMG YLRREADGSW LAEGSVLLRH
     INRKLGLSLP LDGPKTLNGL LLEQFEDIPE AGVSIKLGGV PVEIVQTQDR AVKMARIYPP
     ASDEASSGKP SI
//
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