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Database: UniProt
Entry: A0A1X1MU70_9VIBR
LinkDB: A0A1X1MU70_9VIBR
Original site: A0A1X1MU70_9VIBR 
ID   A0A1X1MU70_9VIBR        Unreviewed;       597 AA.
AC   A0A1X1MU70;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Glutathione-regulated potassium-efflux system protein KefB {ECO:0000256|HAMAP-Rule:MF_01412};
DE   AltName: Full=K(+)/H(+) antiporter {ECO:0000256|HAMAP-Rule:MF_01412};
GN   Name=kefB {ECO:0000256|HAMAP-Rule:MF_01412};
GN   ORFNames=ST37_07940 {ECO:0000313|EMBL:ORT50814.1};
OS   Vibrio sp. qd031.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=1603038 {ECO:0000313|EMBL:ORT50814.1, ECO:0000313|Proteomes:UP000193432};
RN   [1] {ECO:0000313|EMBL:ORT50814.1, ECO:0000313|Proteomes:UP000193432}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=qd031 {ECO:0000313|Proteomes:UP000193432};
RA   Xiang T., Song Y., Huang L., Wang B., Wu P.;
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ORT50814.1, ECO:0000313|Proteomes:UP000193432}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=qd031 {ECO:0000313|Proteomes:UP000193432};
RA   Chen G.;
RT   "Denovo assembling a bacteria genome.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Pore-forming subunit of a potassium efflux system that
CC       confers protection against electrophiles. Catalyzes K(+)/H(+) antiport.
CC       {ECO:0000256|HAMAP-Rule:MF_01412}.
CC   -!- SUBUNIT: Interacts with the regulatory subunit KefG.
CC       {ECO:0000256|HAMAP-Rule:MF_01412}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01412}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01412}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass
CC       membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the monovalent cation:proton antiporter 2 (CPA2)
CC       transporter (TC 2.A.37) family. KefB subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_01412}.
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:ORT50814.1}.
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DR   EMBL; JXQD01000022; ORT50814.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X1MU70; -.
DR   STRING; 1603038.ST37_07940; -.
DR   OrthoDB; 9781411at2; -.
DR   Proteomes; UP000193432; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR   GO; GO:0015503; F:glutathione-regulated potassium exporter activity; IEA:UniProtKB-UniRule.
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   HAMAP; MF_01412; K_H_efflux_KefB; 1.
DR   InterPro; IPR006153; Cation/H_exchanger.
DR   InterPro; IPR004771; K/H_exchanger.
DR   InterPro; IPR020884; K_H_efflux_KefB.
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:SF11; GLUTATHIONE-REGULATED POTASSIUM-EFFLUX SYSTEM PROTEIN KEFB; 1.
DR   PANTHER; PTHR46157; 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   Antiport {ECO:0000256|ARBA:ARBA00022449, ECO:0000256|HAMAP-Rule:MF_01412};
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01412};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01412};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP-
KW   Rule:MF_01412};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01412};
KW   Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|HAMAP-Rule:MF_01412};
KW   Potassium transport {ECO:0000256|ARBA:ARBA00022538, ECO:0000256|HAMAP-
KW   Rule:MF_01412}; Reference proteome {ECO:0000313|Proteomes:UP000193432};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_01412};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_01412};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01412}.
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01412"
FT   TRANSMEM        33..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01412"
FT   TRANSMEM        57..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01412"
FT   TRANSMEM        88..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01412"
FT   TRANSMEM        116..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01412"
FT   TRANSMEM        148..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01412"
FT   TRANSMEM        179..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01412"
FT   TRANSMEM        236..255
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01412"
FT   TRANSMEM        267..287
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01412"
FT   TRANSMEM        293..312
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01412"
FT   TRANSMEM        355..374
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01412"
FT   DOMAIN          400..522
FT                   /note="RCK N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51201"
SQ   SEQUENCE   597 AA;  64955 MW;  413336DA7375C1C6 CRC64;
     MALGNEFLQN SVTFLVAAVA AVPLAQRLGL GSVLGYLLAG VAIGPWGLGL IKDVESILHF
     SEFGVVLLLF LIGLELNPKK LWQMRRPIIG LGGAQVLVTS ALLTGAVSLL GFSWNVSTAI
     AMGLALSSTA IALRVIEEQG LAGSETGQSG FAVLLFQDIA VIPMLALLPV LAGNVAGDWL
     SALSTIAGVL ALLVAGHFLL RPLFRYAIST RTREMFTVTA LLVVVGIAYV MNFMGLSMAL
     GSFLAGVLLA ESEFRHELEI TIEPFKGLLL GLFFMSVGMA VNLGLLALYP LEIFTAVIAL
     VVTKALVLYV LARLFGTRAK ARSKMAAILS QGGEFAFVLY TAAQSQGLLD AETVSFLLVI
     VSLSMVTTPL LLIAQDRWFA RTINEPEFNE PQTVIDKKPR VIVAGFGRFG QIVGRLMYAN
     KVKITILESD ASQIQLLRKY GYKVYYGDAT NLELLRSAGV ETAEAILLCT DSPDEILAIV
     GLCKQHFPHL KVMARARSRV EAYQLINHGV DNFSRETFLG ALDLGRQALI ELGMHPYQAA
     RAEAHFKKLD NRMLEELLPQ HTDDKDLALR AKEARKELEE IFGREMEKDK PQGHDWS
//
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