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NHAP2_SALPK
ID   NHAP2_SALPK             Reviewed;         577 AA.
AC   B5BI52;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 76.
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=SSPA1001;
OS   Salmonella paratyphi A (strain AKU_12601).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=554290;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AKU_12601;
RX   PubMed=19159446; DOI=10.1186/1471-2164-10-36;
RA   Holt K.E., Thomson N.R., Wain J., Langridge G.C., Hasan R., Bhutta Z.A.,
RA   Quail M.A., Norbertczak H., Walker D., Simmonds M., White B., Bason N.,
RA   Mungall K., Dougan G., Parkhill J.;
RT   "Pseudogene accumulation in the evolutionary histories of Salmonella
RT   enterica serovars Paratyphi A and Typhi.";
RL   BMC Genomics 10:36-36(2009).
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; FM200053; CAR59152.1; -; Genomic_DNA.
DR   RefSeq; WP_000338376.1; NC_011147.1.
DR   AlphaFoldDB; B5BI52; -.
DR   SMR; B5BI52; -.
DR   KEGG; sek:SSPA1001; -.
DR   HOGENOM; CLU_005912_9_2_6; -.
DR   OMA; QIGMFVL; -.
DR   Proteomes; UP000001869; 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_1000136715"
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;  62469 MW;  5E6AEDE793BEEC1A CRC64;
     MDAATIISLF ILGSILVTSS ILLSSFSSRL GIPILVIFLA IGMLAGVDGI GGIPFDNYPF
     AYMVSNLALA 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 DNVVRKIGVR VAEDEAE
 
 
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