ID G2H091_9ENTR Unreviewed; 617 AA.
AC G2H091;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
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=Rin_00014710 {ECO:0000313|EMBL:EGY28584.1};
OS Candidatus Regiella insecticola 5.15.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; aphid secondary symbionts; Regiella.
OX NCBI_TaxID=1005043 {ECO:0000313|EMBL:EGY28584.1, ECO:0000313|Proteomes:UP000004116};
RN [1] {ECO:0000313|EMBL:EGY28584.1, ECO:0000313|Proteomes:UP000004116}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R5.15 {ECO:0000313|Proteomes:UP000004116};
RX PubMed=21948522; DOI=10.1101/gr.125351.111;
RA Hansen A.K., Vorburger C., Moran N.A.;
RT "Genomic basis of endosymbiont-conferred protection against an insect
RT parasitoid.";
RL Genome Res. 22:106-114(2012).
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:EGY28584.1}.
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DR EMBL; AGCA01000351; EGY28584.1; -; Genomic_DNA.
DR AlphaFoldDB; G2H091; -.
DR PATRIC; fig|1005043.3.peg.1347; -.
DR Proteomes; UP000004116; 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:UP000004116};
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 20..40
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01412"
FT TRANSMEM 47..66
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01412"
FT TRANSMEM 72..91
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01412"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01412"
FT TRANSMEM 129..151
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01412"
FT TRANSMEM 163..188
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01412"
FT TRANSMEM 200..218
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01412"
FT TRANSMEM 254..270
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01412"
FT TRANSMEM 282..299
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01412"
FT TRANSMEM 305..329
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01412"
FT TRANSMEM 341..360
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01412"
FT TRANSMEM 372..390
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01412"
FT DOMAIN 419..541
FT /note="RCK N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51201"
SQ SEQUENCE 617 AA; 68243 MW; 0D22D1C1C087A73B CRC64;
MVTVPVIHLC IFGEKIMEDS GLLTAILLFL FSAVVAVPIA QRLGIGGVLG YLIAGIAIGP
WGLGFIHDVD EILHFAELGV VFLMFIIGLE LKPAKLWQLR RSIFGVGAGQ VVITALILGA
LLYYSDFAWQ AAIIGGIGLA TSSTAMALQL MREKGMNRNE GGQLGFSVLL FQDIAIIPAL
ALIPLLAGCH GAVENDWGKI SLKMAAFAGM LIGCRYLLRP LFRYIVASGA REVFTAAALL
VVLGSALFMD MLGLSMALGT FIAGVLLAES EFQHELEIAI EPFKGLLLGL FFISVGMALD
VGVLFVHFFI ILMGVIALVS IKIAVLWALS SILTLNRSVR LQFSTVLSQG GEFAFVLFSA
AFSQKVLTAD QLAVLLVVVT LSMMTTPLLM KGIDWMLARR YNEQEENDEK PFVEDNDPQV
IIVGFGRFGQ VIGRLLMANK MRITVLERDV SAVSMMRKYG YKVYYGDATQ LDLLRAAGAE
KAKAIVITCD EPEDTMELVR LCQQYFPNLC IFARARGRVE AHELLQSGVD NFARETFSSA
LELGRKTLLA LGMHPHQAYR VQQHFRRLDM RMLRELMPQH HGDVAQISRV KEARRELEDI
FQRDMQDEQR QFADWDK
//
