ID A0A0J1GFZ0_9GAMM Unreviewed; 608 AA.
AC A0A0J1GFZ0;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
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=ABT58_22695 {ECO:0000313|EMBL:KLU98423.1};
OS Photobacterium aphoticum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=754436 {ECO:0000313|EMBL:KLU98423.1, ECO:0000313|Proteomes:UP000036426};
RN [1] {ECO:0000313|EMBL:KLU98423.1, ECO:0000313|Proteomes:UP000036426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25995 {ECO:0000313|EMBL:KLU98423.1,
RC ECO:0000313|Proteomes:UP000036426};
RA Machado H., Gram L.;
RT "Photobacterium galathea sp. nov.";
RL Submitted (MAY-2015) 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:KLU98423.1}.
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DR EMBL; LDOV01000054; KLU98423.1; -; Genomic_DNA.
DR RefSeq; WP_047876722.1; NZ_PYMF01000176.1.
DR AlphaFoldDB; A0A0J1GFZ0; -.
DR PATRIC; fig|754436.4.peg.4767; -.
DR OrthoDB; 9781411at2; -.
DR Proteomes; UP000036426; 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:UP000036426};
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..24
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01412"
FT TRANSMEM 31..49
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01412"
FT TRANSMEM 55..74
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01412"
FT TRANSMEM 94..115
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01412"
FT TRANSMEM 121..139
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01412"
FT TRANSMEM 151..173
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01412"
FT TRANSMEM 185..203
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01412"
FT TRANSMEM 215..233
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01412"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01412"
FT TRANSMEM 296..315
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01412"
FT TRANSMEM 327..346
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01412"
FT TRANSMEM 358..377
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01412"
FT DOMAIN 404..526
FT /note="RCK N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51201"
SQ SEQUENCE 608 AA; 65918 MW; 862E6B244317D1B2 CRC64;
MASDILSVSV VFLAAAVVAV PIAQRLGLGS VLGYLLAGIA IGPWGLRLID DVDAILHFAE
FGVVLLLFLI GLELNPKKLW QMRKPILGLG GSQVLISTLV IAAIVWACQA FFPAITWRDA
LVVGMGLALS STAIALKVLE EQGLGGSETG QSGFAVLLFQ DIAVIPMLAI LPVLAGGGGG
SWIDLLWMVG GITALLVGGH FLLRPLFRWV VMSGVRELFN VAALLLVVGI ALGMQSLGLS
MALGTFLAGV LLAESEYRHE LEIAIEPFKG LLLGLFFISV GMAVNLGLLV AYPLQILLAV
TALIVVKGLV LYGLARAFGI RAKSRSQMAA ILSQGGEFAF VLFTAALGEG LLGKALSAFL
LVVVSLSMMT TPLILLLQDK WFRYAFEAEE EETLEPDVED RAPRVIITGF GRFGQVVGRL
LFANKIRVTV LERDPGQIQF LRKFGYKVYY GDATQVDLLR AAGADKAEAI IICTDAPDEV
MEVVALCQQY FPHLKVLARA RSRVEAHQLL SHGVESFSRE TFAGALDLGR QALISLGMHP
YQAKRAEAHF RKLDTTALRE LLPQHSEDVH LASRAREARK ELEDIFDREM RGERDRHAGW
DERDDTSG
//
