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NHAP2_SALHS
ID   NHAP2_SALHS             Reviewed;         577 AA.
AC   B4TKD1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=K(+)/H(+) antiporter NhaP2 {ECO:0000255|HAMAP-Rule:MF_01075};
DE   AltName: Full=Potassium/proton antiporter NhaP2 {ECO:0000255|HAMAP-Rule:MF_01075};
GN   Name=nhaP2 {ECO:0000255|HAMAP-Rule:MF_01075}; Synonyms=cvrA;
GN   OrderedLocusNames=SeHA_C1999;
OS   Salmonella heidelberg (strain SL476).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=454169;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SL476;
RX   PubMed=21602358; DOI=10.1128/jb.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(2011).
CC   -!- FUNCTION: K(+)/H(+) antiporter that extrudes potassium in exchange for
CC       external protons and maintains the internal concentration of potassium
CC       under toxic levels. {ECO:0000255|HAMAP-Rule:MF_01075}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+)(out) + K(+)(in) = H(+)(in) + K(+)(out);
CC         Xref=Rhea:RHEA:29467, ChEBI:CHEBI:15378, ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01075};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29468;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01075};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01075}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01075}.
CC   -!- SIMILARITY: Belongs to the monovalent cation:proton antiporter 1 (CPA1)
CC       transporter (TC 2.A.36) family. NhaP2 subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_01075}.
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DR   EMBL; CP001120; ACF66640.1; -; Genomic_DNA.
DR   RefSeq; WP_000338386.1; NC_011083.1.
DR   AlphaFoldDB; B4TKD1; -.
DR   SMR; B4TKD1; -.
DR   KEGG; seh:SeHA_C1999; -.
DR   HOGENOM; CLU_005912_9_2_6; -.
DR   OMA; QIGMFVL; -.
DR   Proteomes; UP000001866; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0015386; F:potassium:proton antiporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006884; P:cell volume homeostasis; IEA:InterPro.
DR   Gene3D; 1.20.1530.20; -; 1.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.30.70.1450; -; 1.
DR   HAMAP; MF_01075; NhaP2; 1.
DR   InterPro; IPR006153; Cation/H_exchanger.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR038770; Na+/solute_symporter_sf.
DR   InterPro; IPR030151; NhaP.
DR   InterPro; IPR023729; NhaP2.
DR   InterPro; IPR006037; RCK_C.
DR   InterPro; IPR036721; RCK_C_sf.
DR   InterPro; IPR005170; Transptr-assoc_dom.
DR   PANTHER; PTHR32507:SF7; PTHR32507:SF7; 1.
DR   Pfam; PF03471; CorC_HlyC; 1.
DR   Pfam; PF00999; Na_H_Exchanger; 1.
DR   Pfam; PF02080; TrkA_C; 1.
DR   SMART; SM01091; CorC_HlyC; 1.
DR   SUPFAM; SSF116726; SSF116726; 1.
DR   SUPFAM; SSF56176; SSF56176; 1.
DR   PROSITE; PS51202; RCK_C; 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..577
FT                   /note="K(+)/H(+) antiporter NhaP2"
FT                   /id="PRO_1000136713"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT   TRANSMEM        30..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT   TRANSMEM        58..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT   TRANSMEM        87..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT   TRANSMEM        109..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT   TRANSMEM        185..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT   TRANSMEM        221..241
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT   TRANSMEM        271..291
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT   TRANSMEM        293..313
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT   TRANSMEM        334..354
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT   TRANSMEM        363..383
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT   DOMAIN          403..485
FT                   /note="RCK C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
SQ   SEQUENCE   577 AA;  62453 MW;  645AEDE78ADA7270 CRC64;
     MDAATIISLF ILGSILVTSS ILLSSFSSRL GIPILVIFLA IGMLAGVDGI GGIPFDNYPF
     TYMVSNLALA IILLDGGMRT QASSFRVALG PALSLATLGV LITSGLTGMM AAWLFHLDLI
     EGLLIGAIVG STDAAAVFSL LGGKGLNERV GSTLEIESGS NDPMAVFLTI TLIEMIQKHE
     TGLDWMFAVH IIQQFGLGIV FGLGGGYLLQ QMINRISLPS GLYPMLALSG GILIFALTTA
     LEGSGILAVY LCGFLLGNRP IRNRYGILQN FDGLAWLAQI AMFLVLGLLV TPSDLWPIAV
     PALILSIWMI FFARPLSVFT GLLPFRGFNL RERIFISWVG LRGAVPIILA VFPMMAGLEN
     ARLFFNVAFF VVLVSLLLQG TSLSWAAKRA KVVVPPVGWP VSRVGLDIHP DNPWEQFIYQ
     LSADKWCVGA ALRDLHMPNE TRIAALFRNN ELFHPTGSTR LQEGDVLCVI GRERDLPALG
     KLFSQSPPVS LDQRFFGDFI LEANAKFADV ALIYGLEEGT EYRDKQQTLG EIIQQLLGAA
     PVVGDQVEFG GMIWTVAEKE DSVVHKIGVR VAEDEAE
 
 
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