ID D8G0Q6_9CYAN Unreviewed; 752 AA.
AC D8G0Q6;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Sodium/hydrogen exchanger {ECO:0000313|EMBL:CBN56196.1};
GN ORFNames=OSCI_2870009 {ECO:0000313|EMBL:CBN56196.1};
OS Kamptonema sp. PCC 6506.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Kamptonema.
OX NCBI_TaxID=272129 {ECO:0000313|EMBL:CBN56196.1, ECO:0000313|Proteomes:UP000004532};
RN [1] {ECO:0000313|Proteomes:UP000004532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6506 {ECO:0000313|Proteomes:UP000004532};
RX PubMed=20675499; DOI=10.1128/JB.00704-10;
RA Mejean A., Mazmouz R., Mann S., Calteau A., Medigue C., Ploux O.;
RT "The genome sequence of the cyanobacterium Oscillatoria sp. PCC 6506
RT reveals several gene clusters responsible for the biosynthesis of toxins
RT and secondary metabolites.";
RL J. Bacteriol. 192:5264-5265(2010).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CACA01000252; CBN56196.1; -; Genomic_DNA.
DR RefSeq; WP_007355408.1; NZ_CACA01000252.1.
DR AlphaFoldDB; D8G0Q6; -.
DR OrthoDB; 9793589at2; -.
DR Proteomes; UP000004532; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015386; F:potassium:proton antiporter activity; IEA:InterPro.
DR Gene3D; 1.20.1530.20; -; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.30.70.1450; Regulator of K+ conductance, C-terminal domain; 2.
DR InterPro; IPR006153; Cation/H_exchanger.
DR InterPro; IPR045158; KEA4/5/6-like.
DR InterPro; IPR038770; Na+/solute_symporter_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR006037; RCK_C.
DR InterPro; IPR036721; RCK_C_sf.
DR InterPro; IPR003148; RCK_N.
DR PANTHER; PTHR16254; POTASSIUM/PROTON ANTIPORTER-RELATED; 1.
DR PANTHER; PTHR16254:SF30; TRANSMEMBRANE AND COILED-COIL DOMAIN-CONTAINING PROTEIN 3; 1.
DR Pfam; PF00999; Na_H_Exchanger; 1.
DR Pfam; PF02080; TrkA_C; 2.
DR Pfam; PF02254; TrkA_N; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF116726; TrkA C-terminal domain-like; 2.
DR PROSITE; PS51202; RCK_C; 2.
DR PROSITE; PS51201; RCK_N; 1.
PE 4: Predicted;
KW Antiport {ECO:0000256|ARBA:ARBA00022449};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000004532};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 33..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 63..81
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 151..173
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 179..209
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 221..254
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 274..292
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 299..321
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 359..381
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 416..538
FT /note="RCK N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51201"
FT DOMAIN 580..665
FT /note="RCK C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51202"
FT DOMAIN 669..748
FT /note="RCK C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51202"
SQ SEQUENCE 752 AA; 81196 MW; 6973B797EA6C3C30 CRC64;
MQEDFRLIVD LVLVLAAAAA GGLFASLLRQ PPLLGYLLGG IVVGPTGLGL IKELIQVETL
AQFGVAFLLF ALGVEFSFAE LNRVKGISLG GGGLQIVLTI VVTTLVSVGM GWVHSPAQGV
FLGAILSLSS TAVVLKCLME RNEAATPHGQ VMLGILVVQD LALGLMLAVL PALNQPAEAI
GMAIASALLR ISLFALGAII VGILVIPPLL RFLAKTESKE LFLLGVVVLA LSIALLTEQL
GFSIEMGAFV AGLMISEVEY ADQTLTYVEP LRDIFASLFF VAVGMLIDPR FLWNNLELIL
GLVFIVFVCK SAIITPIVRS FGYPLKTALI VGLGLAQIGE FSFVLASAGQ NLGLVSRRVY
LLIAGTTAVT LVITPFVMGM VPKLLNWAET FEPLQPYFDQ SSQPTAIAEN LPTQNHVVIC
GYGRVGRNLV RLMQSHGYPV VVIDQSESRV QECRAQNIPY IYGNAGSLHV LEAAGVERAK
AMAIALPDPM STRLSLKRAL ELAPELDIVV RANQDKDIEL LYQLGALEVV QPEFEASLEL
SSHLLEGMGL SAIAIEGEVQ QIRSSRYLEF RPDRQPLEVS RELKVAVKDM NSKWFSLPED
SPLVGMTLEE TNLRQLTGVS LMAIVRNLGE EIDYPHGQTV LQGSDRVLVV GEPEELASFY
LLARGEVALP QGGNSCQWLA VAANSPWGGK KLSELDLANL CGVEVQAIQR EGKFIRWPEG
DIDLQEGDRV LLCGSFYQLG SVHEQIELMV NG
//
