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Database: UniProt
Entry: A7ZSM6
LinkDB: A7ZSM6
Original site: A7ZSM6 
ID   KEFB_ECO24              Reviewed;         601 AA.
AC   A7ZSM6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   RecName: Full=Glutathione-regulated potassium-efflux system protein KefB {ECO:0000255|HAMAP-Rule:MF_01412};
DE   AltName: Full=K(+)/H(+) antiporter {ECO:0000255|HAMAP-Rule:MF_01412};
GN   Name=kefB {ECO:0000255|HAMAP-Rule:MF_01412};
GN   OrderedLocusNames=EcE24377A_3820;
OS   Escherichia coli O139:H28 (strain E24377A / ETEC).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331111;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E24377A / ETEC;
RX   PubMed=18676672; DOI=10.1128/jb.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic analysis
RT   of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
CC   -!- FUNCTION: Pore-forming subunit of a potassium efflux system that
CC       confers protection against electrophiles. Catalyzes K(+)/H(+) antiport.
CC       {ECO:0000255|HAMAP-Rule:MF_01412}.
CC   -!- SUBUNIT: Interacts with the regulatory subunit KefG.
CC       {ECO:0000255|HAMAP-Rule:MF_01412}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01412}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01412}.
CC   -!- SIMILARITY: Belongs to the monovalent cation:proton antiporter 2 (CPA2)
CC       transporter (TC 2.A.37) family. KefB subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_01412}.
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DR   EMBL; CP000800; ABV16918.1; -; Genomic_DNA.
DR   RefSeq; WP_000399129.1; NC_009801.1.
DR   AlphaFoldDB; A7ZSM6; -.
DR   SMR; A7ZSM6; -.
DR   KEGG; ecw:EcE24377A_3820; -.
DR   HOGENOM; CLU_005126_9_3_6; -.
DR   Proteomes; UP000001122; Chromosome.
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; Cell inner membrane; Cell membrane; Ion transport; Membrane;
KW   Potassium; Potassium transport; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..601
FT                   /note="Glutathione-regulated potassium-efflux system
FT                   protein KefB"
FT                   /id="PRO_1000068454"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01412"
FT   TRANSMEM        29..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01412"
FT   TRANSMEM        55..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01412"
FT   TRANSMEM        87..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01412"
FT   TRANSMEM        115..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01412"
FT   TRANSMEM        152..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01412"
FT   TRANSMEM        177..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01412"
FT   TRANSMEM        207..227
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01412"
FT   TRANSMEM        230..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01412"
FT   TRANSMEM        268..288
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01412"
FT   TRANSMEM        291..311
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01412"
FT   TRANSMEM        324..344
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01412"
FT   TRANSMEM        356..376
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01412"
FT   DOMAIN          402..524
FT                   /note="RCK N-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01412"
SQ   SEQUENCE   601 AA;  66395 MW;  A84CA345747B84C0 CRC64;
     MEGSDFLLAG VLFLFAAVAA VPLASRLGIG AVLGYLLAGI AIGPWGLGFI SDVDEILHFS
     ELGVVFLMFI IGLELNPSKL WQLRRSIFGV GAAQVLLSAA LLAGLLMLTD FAWQAAVVGG
     IGLAMSSTAM ALQLMREKGM NRSESGQLGF SVLLFQDLAV IPALALVPLL AGSADEHFDW
     MKIGMKVLAF VGMLIGGRYL LRPVFRFIAA SGVREVFTAA TLLLVLGSAL FMDALGLSMA
     LGTFIAGVLL AESEYRHELE TAIDPFKGLL LGLFFISVGM SLNLGVLYTH LLWVVISVVV
     LVAVKILVLY LLARLYGVRS SERMQFAGVL SQGGEFAFVL FSTASSQRLF QGDQMALLLV
     TVTLSMMTTP LLMKLVDKWL SRQFNGPEEE DEKPWVNDDK PQVIVVGFGR FGQVIGRLLM
     ANKMRITVLE RDISAVNLMR KYGYKVYYGD ATQVDLLRSA GAEAAVSIVI TCNEPEDTMK
     LVEICQQHFP HLHILARARG RVEAHELLQA GVTQFSRETF SSALELGRKT LVTLGMHPHQ
     AQRAQLHFRR LDMRMLRELI PMHADTVQIS RAREARRELE EIFQREMQQE RRQLDGWDEF
     E
//
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