ID A6D761_9VIBR Unreviewed; 598 AA.
AC A6D761;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 82.
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=VSAK1_09258 {ECO:0000313|EMBL:EDL51545.1};
OS Vibrio mediterranei AK1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=391591 {ECO:0000313|EMBL:EDL51545.1, ECO:0000313|Proteomes:UP000003769};
RN [1] {ECO:0000313|EMBL:EDL51545.1, ECO:0000313|Proteomes:UP000003769}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK1 {ECO:0000313|EMBL:EDL51545.1,
RC ECO:0000313|Proteomes:UP000003769};
RA Rosenberg E., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUN-2007) 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:EDL51545.1}.
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DR EMBL; ABCH01000054; EDL51545.1; -; Genomic_DNA.
DR RefSeq; WP_006074808.1; NZ_ABCH01000054.1.
DR AlphaFoldDB; A6D761; -.
DR Proteomes; UP000003769; 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; IPR006036; K_uptake_TrkA.
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 PRINTS; PR00335; KUPTAKETRKA.
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};
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 148..170
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01412"
FT TRANSMEM 182..200
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01412"
FT TRANSMEM 212..230
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..315
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01412"
FT TRANSMEM 327..349
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01412"
FT TRANSMEM 355..373
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01412"
FT DOMAIN 401..523
FT /note="RCK N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51201"
SQ SEQUENCE 598 AA; 65172 MW; E4E1EDF29EE751D1 CRC64;
MAMTNDFLQS GVIFLSAAVV AVPIAQRLGL GSVLGYLLAG VAIGPWGLGL ISDVDEILHF
SEFGVVLLLF LIGLELNPKK LWQMRVPILG LGGAQVVVTT LILSAIASLF NLSWQTSLAI
GMGLALSSTA IALRVIEEQG LGGGETGQSG FAVLLFQDIA VIPMLALLPL LAGNTAGNWA
DIIWMLAGVL GLLVGGHFLI RPLFRYVVMS GVRELFTVAA LLLVIGIAAF MQKLGLSMAL
GTFLAGVLLA ESEYRHELEI AIEPFKGLLL GLFFIAVGMA VNLGLLISEP LAVLFAVVSL
VIIKGLILYV LARLFGIGPK SRSKMAAILS QGGEFAFVIF TAASAQGLLP AEESAFLLVV
VSLSMVTTPL LLMGQKKWFE KSLNHVEETT IKTDVEDRQP RVIIAGFGRF GQIVGRLMYA
NKVKVTVLES DASQIHLLRK YGYKVFYGDA TQVDLLRAAG ADKAEAIIIC TDSPEEIMEV
VDLCHNHFPK LRVLARARSR VEAYQLMNHG VQCYSRETFL GALDLGRQAL VELGFHPYEA
KRAEAHFRKL DNAMLKELLP QHSEDKELAQ RSKEARKELE EIFGREMEND RQSRNFWD
//
