ID M6RFZ6_LEPIR Unreviewed; 492 AA.
AC M6RFZ6;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Transporter, CPA2 family {ECO:0000313|EMBL:EMO04701.1};
GN ORFNames=LEP1GSC116_2160 {ECO:0000313|EMBL:EMO04701.1};
OS Leptospira interrogans serovar Icterohaemorrhagiae str. Verdun HP.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1049910 {ECO:0000313|EMBL:EMO04701.1, ECO:0000313|Proteomes:UP000012092};
RN [1] {ECO:0000313|EMBL:EMO04701.1, ECO:0000313|Proteomes:UP000012092}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Verdun HP {ECO:0000313|EMBL:EMO04701.1,
RC ECO:0000313|Proteomes:UP000012092};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA Sanka R., DePew J., Purushe J., Picardeau M., Werts C., Goarant C.,
RA Vinetz J.M., Sutton G.G., Nierman W.C., Fouts D.E.;
RL Submitted (JAN-2013) 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}.
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:EMO04701.1}.
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DR EMBL; AHNZ02000598; EMO04701.1; -; Genomic_DNA.
DR AlphaFoldDB; M6RFZ6; -.
DR Proteomes; UP000012092; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR GO; GO:0008324; F:monoatomic cation transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006813; P:potassium ion transport; IEA:UniProtKB-KW.
DR GO; GO:1902600; P:proton transmembrane transport; IEA:InterPro.
DR Gene3D; 1.20.1530.20; -; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR006153; Cation/H_exchanger.
DR InterPro; IPR004771; K/H_exchanger.
DR InterPro; IPR038770; Na+/solute_symporter_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR003148; RCK_N.
DR NCBIfam; TIGR00932; 2a37; 1.
DR PANTHER; PTHR46157; K(+) EFFLUX ANTIPORTER 3, CHLOROPLASTIC; 1.
DR PANTHER; PTHR46157:SF4; K(+) EFFLUX ANTIPORTER 3, CHLOROPLASTIC; 1.
DR Pfam; PF00999; Na_H_Exchanger; 1.
DR Pfam; PF02254; TrkA_N; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS51201; RCK_N; 1.
PE 3: Inferred from homology;
KW Ion transport {ECO:0000256|ARBA:ARBA00022538};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Potassium {ECO:0000256|ARBA:ARBA00022958};
KW Potassium transport {ECO:0000256|ARBA:ARBA00022538};
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..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 32..50
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 56..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 87..110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 148..170
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 186..204
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 216..234
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 270..288
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 294..315
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 336..354
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 360..378
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 403..492
FT /note="RCK N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51201"
SQ SEQUENCE 492 AA; 53471 MW; 708E9D5E4DF7FC01 CRC64;
MLDHNLLINL IVFLSAAVIS VPLFKKIGLG SVVGYLVGGT IIGPWGIGLI TDVDSILHLS
EFGVVLLLFL IGLELKPQRL WILRRPVFGL GGLQVILTSL TFFILFSLLG LEKRQAIVIS
ISISLSSTAF ALQVLGEKNE LNTTHGRSAF AILLFQDLAI IPIMATLSFL TESSSNPGSH
GSIKEILFPI GTIIAVILAG RFLARPLFKL VASSANHEIF TALSLLIVIG VSILMNQVGL
SMALGSFLGG VILADSEYRH ELESNLEPFK GLFLGLFFLA VGMSINLGEV LKDPILVILL
AFILILVKTI ILYFIGIITK HSKEVSLNLS TIISQGGEFA FVILGVGVSL SILPKERADL
VIAVVTLSMG LTPILGILKD KTSKWILKED QNIKEDTIEE QNRVIVAGFG RFGQIIARML
FVHKIGFTAL EHNPDQVNLA RKFGYKIYYG DASKLSLLRS AGAEHADLFI LAIQDIDVSV
KIAELIKKIS RI
//
