ID A0A1T5NWA2_9BACT Unreviewed; 746 AA.
AC A0A1T5NWA2;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Monovalent cation:H+ antiporter-2, CPA2 family {ECO:0000313|EMBL:SKD04745.1};
GN ORFNames=SAMN05660461_2922 {ECO:0000313|EMBL:SKD04745.1};
OS Chitinophaga ginsengisegetis.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=393003 {ECO:0000313|EMBL:SKD04745.1, ECO:0000313|Proteomes:UP000190166};
RN [1] {ECO:0000313|EMBL:SKD04745.1, ECO:0000313|Proteomes:UP000190166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18108 {ECO:0000313|EMBL:SKD04745.1,
RC ECO:0000313|Proteomes:UP000190166};
RA Peterson S.W.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the monovalent cation:proton antiporter 2 (CPA2)
CC transporter (TC 2.A.37) family. {ECO:0000256|ARBA:ARBA00005551}.
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DR EMBL; FUZZ01000002; SKD04745.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T5NWA2; -.
DR STRING; 393003.SAMN05660461_2922; -.
DR Proteomes; UP000190166; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015297; F:antiporter activity; IEA:InterPro.
DR GO; GO:0008324; F:monoatomic cation transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006813; P:potassium ion transport; IEA:InterPro.
DR GO; GO:1902600; P:proton transmembrane transport; IEA:InterPro.
DR Gene3D; 1.20.1530.20; -; 1.
DR Gene3D; 3.30.70.1450; Regulator of K+ conductance, C-terminal domain; 2.
DR InterPro; IPR006153; Cation/H_exchanger.
DR InterPro; IPR038770; Na+/solute_symporter_sf.
DR InterPro; IPR006037; RCK_C.
DR InterPro; IPR036721; RCK_C_sf.
DR PANTHER; PTHR42751:SF3; NA(+)_H(+) ANTIPORTER; 1.
DR PANTHER; PTHR42751; SODIUM/HYDROGEN EXCHANGER FAMILY/TRKA DOMAIN PROTEIN; 1.
DR Pfam; PF00999; Na_H_Exchanger; 1.
DR Pfam; PF02080; TrkA_C; 2.
DR SUPFAM; SSF116726; TrkA C-terminal domain-like; 2.
DR PROSITE; PS51202; RCK_C; 2.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000190166};
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..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 31..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 61..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 190..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 266..286
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 298..320
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 340..368
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 425..444
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 456..478
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 499..520
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 526..544
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 576..660
FT /note="RCK C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51202"
FT DOMAIN 664..746
FT /note="RCK C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51202"
SQ SEQUENCE 746 AA; 82640 MW; 9FEFC3CAD752E55F CRC64;
MHLPSLIIDL ALILGAAGVI TLLFKRLKQP MVLGYIIAGF IVGPNFKLFP TIGDAEGIKT
WSEIGVIFLL FSLGLEFSFK KLMRVGGTAT ITAFVEIALI TVAGYFTGKL MGWGFMDSLF
LGGLLASSST TIIIRAFEEL GIKKKSFTKI VFGVLVIEDI VVILMMVLLS TMAVSRKFEG
TEMLFTIAKL MFFLAVWFLA GIFLLPTALK KIERYLNGET LLILSIALCL GMVILATKVG
FSAELGAFIM GSIIAETTSS EKVEHLIQPV KDLFGAIFFV SVGMLINPEM IIEYRWPVLW
ITLLTITGKF FSTTMGALLS GQPLKQAVQV GMSMAQVGEF AFIIATLGLS LGVTSEFLFP
VAVGVSAITT FTTPYMIKFS IPFYNWLEKI IPARWMATLN RYSASSQTLQ AESDWRIVLR
SYVKVIVLNA VIILAVILLN TYYIGPFVIK YVKNLFLAEL VSVIIGIAMM SPFIWALMVQ
KISSNSYKAL WLDSKYNHGP LVVVEVVRNV VAVLLVGFLV NQYFPFWQAL MGTAIILACV
LLVLRSQLQK YYNRIESRFL TNLNARETAD AANNKATAAD LLPWDAQVSE VEIDPWSTLV
DKPLIDLQLR EKYGINVGAI KRGNVTIYAP TRDEKLFPHD ILTAIGTEAQ LEEFNRVVNT
LNVERSDDVA DENIGLTSIV VDEHNGLKGQ TIRGSGIREK TQALVVGIAR GGEKILNPAS
ETEFEWEDVV WLVGNRRKIL EFSRGR
//
