KEFB_SHIFL
ID KEFB_SHIFL Reviewed; 557 AA.
AC Q83PY0;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 131.
DE RecName: Full=Putative glutathione-regulated potassium-efflux system protein KefB;
DE AltName: Full=K(+)/H(+) antiporter {ECO:0000255|HAMAP-Rule:MF_01412};
GN Name=kefB {ECO:0000255|HAMAP-Rule:MF_01412};
GN OrderedLocusNames=SF3369, S4394;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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}.
CC -!- CAUTION: Could be the product of a pseudogene. Is truncated in the N-
CC terminal where it lacks 31 residues compared to orthologs and it has a
CC 13 residues deletion in between Ala-325 and Pro-326. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN44832.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAP19346.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE005674; AAN44832.2; ALT_INIT; Genomic_DNA.
DR EMBL; AE014073; AAP19346.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q83PY0; -.
DR SMR; Q83PY0; -.
DR STRING; 198214.SF3369; -.
DR EnsemblBacteria; AAN44832; AAN44832; SF3369.
DR EnsemblBacteria; AAP19346; AAP19346; S4394.
DR KEGG; sft:NCTC1_03649; -.
DR KEGG; sfx:S4394; -.
DR PATRIC; fig|623.156.peg.1867; -.
DR HOGENOM; CLU_005126_9_3_6; -.
DR OrthoDB; 941006at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0015503; F:glutathione-regulated potassium exporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0015299; F:solute:proton antiporter activity; IEA:InterPro.
DR Gene3D; 1.20.1530.20; -; 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 Pfam; PF00999; Na_H_Exchanger; 1.
DR Pfam; PF02254; TrkA_N; 1.
DR PRINTS; PR00335; KUPTAKETRKA.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR00932; 2a37; 1.
DR PROSITE; PS51201; RCK_N; 1.
PE 5: Uncertain;
KW Antiport; Cell inner membrane; Cell membrane; Ion transport; Membrane;
KW Potassium; Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..557
FT /note="Putative glutathione-regulated potassium-efflux
FT system protein KefB"
FT /id="PRO_0000196603"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01412"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01412"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01412"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01412"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01412"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01412"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01412"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01412"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01412"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01412"
FT DOMAIN 358..480
FT /note="RCK N-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01412"
SQ SEQUENCE 557 AA; 62085 MW; EB9A2FCEF9F3C19F CRC64;
MLGYLLAGIA IGPWGLGFIS DVDEILHFSE LGVVFLMFII GLELNPSKLW QLRRSIFGVG
AAQVLLSAAL LAGLLMLTDF AWQAAVVGGI GFAMSSTAMA LQLMREKGMN RSESGQLGFS
VLLFQDLAVI PALALVPLLA GSADEHFDWM KIGMKVLEFV GMLIGGRYLL RPVFRFIAAS
GVREVFTAAT LLLVLGSALF MDALGLSMAL GTFIAGVLLA ESEYRHELET AIDPFKGLLL
GLFFISVGMS LNLGVLYTHL LWVVISVVVL VAVKILVLYL LARLYGVRSS ERMQFAGVLS
QGGEFAFVLF STASSQRLFQ GDQMAPLLMK LVDKWLSRQF NGPEEEDEKP WVNDDKPQVI
VVGFGRFGQV IGRLLMANKM RITVLERDIS AVNLMRKYGY KVYYGDATQV DLLRSAGAEA
AESIVITCNE PEDTMKLVEI CQQHFPHLHI LARARGRVEA HELLQAGVTQ FSRETFSSAL
ELGRKTLVTL GMHPHQAQRA QLHFRRLDMR MLRELIPMHA DTVQISRARE ARRELEEIFQ
REMQQERRQL DGWDEFE
