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KEFB_PECCP
ID   KEFB_PECCP              Reviewed;         603 AA.
AC   C6DG97;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   25-MAY-2022, entry version 74.
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}; OrderedLocusNames=PC1_3845;
OS   Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=561230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PC1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA   Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Balakrishnan V., Glasner J., Perna N.T.;
RT   "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL   Submitted (JUL-2009) 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: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; CP001657; ACT14860.1; -; Genomic_DNA.
DR   RefSeq; WP_015841945.1; NC_012917.1.
DR   AlphaFoldDB; C6DG97; -.
DR   SMR; C6DG97; -.
DR   STRING; 561230.PC1_3845; -.
DR   EnsemblBacteria; ACT14860; ACT14860; PC1_3845.
DR   KEGG; pct:PC1_3845; -.
DR   eggNOG; COG0475; Bacteria.
DR   eggNOG; COG1226; Bacteria.
DR   HOGENOM; CLU_005126_9_3_6; -.
DR   OMA; IRPFHDV; -.
DR   OrthoDB; 941006at2; -.
DR   Proteomes; UP000002736; 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; 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   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR00932; 2a37; 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; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..603
FT                   /note="Glutathione-regulated potassium-efflux system
FT                   protein KefB"
FT                   /id="PRO_1000215223"
FT   TRANSMEM        5..25
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        180..202
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        326..346
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   603 AA;  66573 MW;  F1EC6D2D1783A82B CRC64;
     MESSALLTAG VLFLFVAVVA VPIAARLGIG AVLGYLIAGI AIGPWGLGFI RDVDAILHFS
     ELGVVFLMFI IGLELNPSKL WTLRRSIFGV GAAQVGLSTL LLGGALYLTD FSWQSALIGG
     VGLAMSSTAM ALQLMREKGM NRSESGQLGF SVLLFQDLAV IPALALIPIL AGVQGDFGDW
     ERIGLKVAAF LGMLIGGRYL VRPLFRFIAA SGVREVFTAA ALLLVLGSAL FMETLGLSMA
     LGTFIAGILL AESEYRHELE IAIEPFKGLL LGLFFISVGM ALNLGILYTH IVKIMVAVLV
     LVAVKAAVLY FLARVNRMRR SERLQFAGVL SQGGEFAFVL FSAAASFNVL KGEQLPLLLV
     TVTLSMMTTP LLMQLIDRIL ARRYNVQDVP DEKPYVEDDE PQVIVVGFGR FGQVISRLLM
     ANKMRITVLE RDISAVSLMR SYGYKVYYGD ATELELLRSA GADKARSIVI TCNAPEDTME
     IVHLCQQHFP NLEILARARG RVEAHELLQT GVRHFSRETF SSALELGRKT LVTLGMHPHQ
     AMRAQQHFRR LDMRMLRELM PQLTGDVAQI SRVKEARREL EDIFQREMQR ERRRPSVWDE
     DDE
 
 
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