NAH1_METJA
ID NAH1_METJA Reviewed; 426 AA.
AC Q60362;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 127.
DE RecName: Full=Na(+)/H(+) antiporter 1;
DE AltName: Full=MjNhaP1;
GN OrderedLocusNames=MJ0057;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP FUNCTION.
RX PubMed=12220668; DOI=10.1016/s0014-5793(02)03244-1;
RA Hellmer J., Paetzold R., Zeilinger C.;
RT "Identification of a pH regulated Na(+)/H(+) antiporter of Methanococcus
RT jannaschii.";
RL FEBS Lett. 527:245-249(2002).
RN [3]
RP MUTAGENESIS OF ASP-93; ASP-132; GLU-156; ASP-161; HIS-211; HIS-215;
RP ARG-320; HIS-333 AND ARG-347.
RX PubMed=12729893; DOI=10.1016/s0014-5793(03)00332-6;
RA Hellmer J., Teubner A., Zeilinger C.;
RT "Conserved arginine and aspartate residues are critical for function of
RT MjNhaP1, a Na+/H+ antiporter of M. jannaschii.";
RL FEBS Lett. 542:32-36(2003).
CC -!- FUNCTION: This is a Na(+)/H(+) antiporter. Can also transport lithium.
CC {ECO:0000269|PubMed:12220668}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Active at pH 7.0 and below.;
CC -!- INTERACTION:
CC Q60362; Q60362: MJ0057; NbExp=2; IntAct=EBI-8539024, EBI-8539024;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
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; L77117; AAB98037.1; -; Genomic_DNA.
DR PIR; A64307; A64307.
DR RefSeq; WP_010869549.1; NC_000909.1.
DR PDB; 4CZB; X-ray; 3.50 A; A/B/C/D=1-426.
DR PDB; 4D0A; EM; 6.00 A; B=1-426.
DR PDBsum; 4CZB; -.
DR PDBsum; 4D0A; -.
DR AlphaFoldDB; Q60362; -.
DR SMR; Q60362; -.
DR MINT; Q60362; -.
DR STRING; 243232.MJ_0057; -.
DR TCDB; 2.A.36.6.6; the monovalent cation:proton antiporter-1 (cpa1) family.
DR EnsemblBacteria; AAB98037; AAB98037; MJ_0057.
DR GeneID; 1450896; -.
DR KEGG; mja:MJ_0057; -.
DR eggNOG; arCOG01961; Archaea.
DR HOGENOM; CLU_005912_9_3_2; -.
DR InParanoid; Q60362; -.
DR OMA; KWEGILI; -.
DR OrthoDB; 47913at2157; -.
DR PhylomeDB; Q60362; -.
DR Proteomes; UP000000805; Chromosome.
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:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0015299; F:solute:proton antiporter activity; IEA:InterPro.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1530.20; -; 1.
DR InterPro; IPR006153; Cation/H_exchanger.
DR InterPro; IPR038770; Na+/solute_symporter_sf.
DR Pfam; PF00999; Na_H_Exchanger; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiport; Cell membrane; Ion transport; Membrane;
KW Reference proteome; Sodium; Sodium transport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..426
FT /note="Na(+)/H(+) antiporter 1"
FT /id="PRO_0000052402"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MUTAGEN 93
FT /note="D->A: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:12729893"
FT MUTAGEN 132
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:12729893"
FT MUTAGEN 156
FT /note="E->A: Almost no change in activity."
FT /evidence="ECO:0000269|PubMed:12729893"
FT MUTAGEN 161
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:12729893"
FT MUTAGEN 211
FT /note="H->R: No change in activity; when associated with R-
FT 215."
FT /evidence="ECO:0000269|PubMed:12729893"
FT MUTAGEN 215
FT /note="H->R: No change in activity; when associated with R-
FT 211."
FT /evidence="ECO:0000269|PubMed:12729893"
FT MUTAGEN 320
FT /note="R->A,D: Loss of activity."
FT /evidence="ECO:0000269|PubMed:12729893"
FT MUTAGEN 320
FT /note="R->H: Almost no change in activity."
FT /evidence="ECO:0000269|PubMed:12729893"
FT MUTAGEN 333
FT /note="H->R: No change in activity."
FT /evidence="ECO:0000269|PubMed:12729893"
FT MUTAGEN 347
FT /note="R->A: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:12729893"
FT HELIX 2..26
FT /evidence="ECO:0007829|PDB:4CZB"
FT HELIX 32..42
FT /evidence="ECO:0007829|PDB:4CZB"
FT TURN 43..46
FT /evidence="ECO:0007829|PDB:4CZB"
FT HELIX 51..76
FT /evidence="ECO:0007829|PDB:4CZB"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:4CZB"
FT HELIX 86..93
FT /evidence="ECO:0007829|PDB:4CZB"
FT HELIX 95..111
FT /evidence="ECO:0007829|PDB:4CZB"
FT HELIX 119..128
FT /evidence="ECO:0007829|PDB:4CZB"
FT TURN 133..136
FT /evidence="ECO:0007829|PDB:4CZB"
FT HELIX 137..140
FT /evidence="ECO:0007829|PDB:4CZB"
FT TURN 141..144
FT /evidence="ECO:0007829|PDB:4CZB"
FT HELIX 147..174
FT /evidence="ECO:0007829|PDB:4CZB"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:4CZB"
FT HELIX 183..211
FT /evidence="ECO:0007829|PDB:4CZB"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:4CZB"
FT HELIX 218..233
FT /evidence="ECO:0007829|PDB:4CZB"
FT HELIX 236..240
FT /evidence="ECO:0007829|PDB:4CZB"
FT HELIX 248..264
FT /evidence="ECO:0007829|PDB:4CZB"
FT HELIX 269..295
FT /evidence="ECO:0007829|PDB:4CZB"
FT HELIX 298..317
FT /evidence="ECO:0007829|PDB:4CZB"
FT HELIX 319..327
FT /evidence="ECO:0007829|PDB:4CZB"
FT HELIX 335..343
FT /evidence="ECO:0007829|PDB:4CZB"
FT HELIX 349..364
FT /evidence="ECO:0007829|PDB:4CZB"
FT STRAND 368..371
FT /evidence="ECO:0007829|PDB:4CZB"
FT TURN 372..376
FT /evidence="ECO:0007829|PDB:4CZB"
FT HELIX 379..410
FT /evidence="ECO:0007829|PDB:4CZB"
SQ SEQUENCE 426 AA; 45966 MW; 967F9A3E60949A1D CRC64;
MELMMAIGYL GLALVLGSLV AKIAEKLKIP DIPLLLLLGL IIGPFLQIIP SDSAMEIFEY
AGPIGLIFIL LGGAFTMRIS LLKRVIKTVV RLDTITFLIT LLISGFIFNM VLNLPYTSPV
GYLFGAITAA TDPATLIPVF SRVRTNPEVA ITLEAESIFN DPLGIVSTSV ILGLFGLFSS
SNPLIDLITL AGGAIVVGLL LAKIYEKIII HCDFHEYVAP LVLGGAMLLL YVGDDLLPSI
CGYGFSGYMA VAIMGLYLGD ALFRADDIDY KYIVSFCDDL SLLARVFIFV FLGACIKLSM
LENYFIPGLL VALGSIFLAR PLGVFLGLIG SKHSFKEKLY FALEGPRGVV PAALAVTVGI
EILKNADKIP ASITKYITPT DIAGTIIIGT FMTILLSVIL EASWAGMLAL KLLGEYKPKY
KEESHH
