NHAP_ALKAM
ID NHAP_ALKAM Reviewed; 574 AA.
AC Q0ZAH6;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=K(+)/H(+) antiporter NhaP;
DE AltName: Full=Potassium/proton antiporter NhaP;
GN Name=nhaP;
OS Alkalimonas amylolytica.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alkalimonas.
OX NCBI_TaxID=152573;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP AND GENE NAME.
RC STRAIN=N10;
RX PubMed=17600061; DOI=10.1099/mic.0.2007/007450-0;
RA Wei Y., Liu J., Ma Y., Krulwich T.A.;
RT "Three putative cation/proton antiporters from the soda lake alkaliphile
RT Alkalimonas amylolytica N10 complement an alkali-sensitive Escherichia coli
RT mutant.";
RL Microbiology 153:2168-2179(2007).
CC -!- FUNCTION: K(+)/H(+) antiporter that extrudes potassium in exchange for
CC external protons. Can also catalyze NH(4)(+)/H(+) antiport. Could have
CC weak activity with Na(+). {ECO:0000269|PubMed:17600061}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.5 mM for K(+) (at pH 8.0) {ECO:0000269|PubMed:17600061};
CC pH dependence:
CC Optimum pH is 7.5. Exhibits K(+)/H(+) antiporter activity between pH
CC 7.5 and 9.5. {ECO:0000269|PubMed:17600061};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the monovalent cation:proton antiporter 1 (CPA1)
CC transporter (TC 2.A.36) family. {ECO:0000305}.
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DR EMBL; DQ649020; ABG37987.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0ZAH6; -.
DR SMR; Q0ZAH6; -.
DR STRING; 152573.SAMN04488051_11215; -.
DR TCDB; 2.A.36.6.4; the monovalent cation:proton antiporter-1 (cpa1) family.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0005451; F:monovalent cation:proton antiporter activity; IEA:InterPro.
DR GO; GO:0006813; P:potassium ion transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1530.20; -; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.1450; -; 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; 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 SMART; SM01091; CorC_HlyC; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR PROSITE; PS51202; RCK_C; 1.
PE 1: Evidence at protein level;
KW Antiport; Cell inner membrane; Cell membrane; Ion transport; Membrane;
KW Potassium; Potassium transport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..574
FT /note="K(+)/H(+) antiporter NhaP"
FT /id="PRO_0000423860"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 272..292
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 332..352
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..381
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 402..484
FT /note="RCK C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00544"
SQ SEQUENCE 574 AA; 62268 MW; 2C94817C6A0956F6 CRC64;
MEAINLTILV IGVLFLISIV ATLISSRIGA PILLVFLIIG MLAGEQGLGG ITFNNPQVAF
LIGSIALVII LFDGGMRTHP ERFRVALAPA AMLATLGVVV TCTVTGLAAA WILGLHWLQG
LLLGAILSST DAAAVFSIFQ SRGIRIKDRV ASTLEIESGS NDPMAVMLTI TLVGVLAEYT
ALDWSVLIVF LKQAIIGGAV GYGAGRLFVF LCRKLPLSFA FFPLMAVACC ISVYAVTTQF
EGSGFLAVYL MGYFVGNARL PQVLYILRVH DGLAWLSQIV MFLMLGLLVV PSQLLDHLLP
ALAIAGVLIF IARPLAVLLS LIPFHFPAKD QLFISWVGLR GAVPIILALF PWLAGVPDEH
LYFNVAFVIV IVSLVFQGWS ISPVARWLKL EVPKESGPDQ TMPLDAIASN EVIEVVSFTL
KGDSPMLDKQ WQDFTVPHSA EFLGVIRDGE WLLSRDNPVF KLKDSVLVLC KMADVPDIST
VLASAASSRT MTASDFFGDF VLNAQITLDE LDAFYSITLP EHESHVTLAD YITERFHRRV
VVGDQVKLDA LVLTVRQLDD HGNVKLVGIK PSDS