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K( )-stimulated pyrophosphate-energized sodium pump (EC 3.6.1.1) (Membrane-bound sodium-translocating pyrophosphatase) (Pyrophosphate-energized inorganic pyrophosphatase) (Na( )-PPase) (Tm-PPase)

 HPPA_THEMA              Reviewed;         726 AA.
Q9S5X0; O51935;
25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
27-SEP-2017, entry version 116.
RecName: Full=K(+)-stimulated pyrophosphate-energized sodium pump;
EC=3.6.1.1 {ECO:0000255|HAMAP-Rule:MF_01129};
AltName: Full=Membrane-bound sodium-translocating pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01129};
AltName: Full=Pyrophosphate-energized inorganic pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01129};
Short=Na(+)-PPase {ECO:0000255|HAMAP-Rule:MF_01129};
AltName: Full=Tm-PPase;
Name=hppA {ECO:0000255|HAMAP-Rule:MF_01129};
OrderedLocusNames=TM_0174;
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099).
Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
NCBI_TaxID=243274;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099;
PubMed=10360571; DOI=10.1038/20601;
Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J.,
Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A.,
McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M.,
Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L.,
Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O.,
Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.;
"Evidence for lateral gene transfer between Archaea and Bacteria from
genome sequence of Thermotoga maritima.";
Nature 399:323-329(1999).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-276.
STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099;
PubMed=9440516;
Bouthier de la Tour C., Portemer C., Kaltoum H., Duguet M.;
"Reverse gyrase from the hyperthermophilic bacterium Thermotoga
maritima: properties and gene structure.";
J. Bacteriol. 180:274-281(1998).
[3]
CHARACTERIZATION, FUNCTION, COFACTOR, ENZYME REGULATION, AND
BIOPHYSICOCHEMICAL PROPERTIES.
STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099;
PubMed=11343697; DOI=10.1016/S0014-5793(01)02390-0;
Perez-Castineira J.R., Lopez-Marques R.L., Losada M., Serrano A.;
"A thermostable K(+)-stimulated vacuolar-type pyrophosphatase from the
hyperthermophilic bacterium Thermotoga maritima.";
FEBS Lett. 496:6-11(2001).
[4]
CATALYTIC ACTIVITY, ENZYME REGULATION, AND MUTAGENESIS OF ASP-190 AND
ASP-703.
PubMed=15697234; DOI=10.1021/bi048429g;
Belogurov G.A., Malinen A.M., Turkina M.V., Jalonen U., Rytkonen K.,
Baykov A.A., Lahti R.;
"Membrane-bound pyrophosphatase of Thermotoga maritima requires sodium
for activity.";
Biochemistry 44:2088-2096(2005).
[5]
SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=16182234; DOI=10.1016/j.bbamem.2005.08.004;
Lopez-Marques R.L., Perez-Castineira J.R., Buch-Pedersen M.J.,
Marco S., Rigaud J.L., Palmgren M.G., Serrano A.;
"Large-scale purification of the proton pumping pyrophosphatase from
Thermotoga maritima: a 'Hot-Solve' method for isolation of recombinant
thermophilic membrane proteins.";
Biochim. Biophys. Acta 1716:69-76(2005).
[6]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=17605473; DOI=10.1021/bi700564b;
Malinen A.M., Belogurov G.A., Baykov A.A., Lahti R.;
"Na+-pyrophosphatase: a novel primary sodium pump.";
Biochemistry 46:8872-8878(2007).
[7]
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH CALCIUM AND
MAGNESIUM, TOPOLOGY, FUNCTION, SUBUNIT, METAL-BINDING SITES, ENZYME
REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=22837527; DOI=10.1126/science.1222505;
Kellosalo J., Kajander T., Kogan K., Pokharel K., Goldman A.;
"The structure and catalytic cycle of a sodium-pumping
pyrophosphatase.";
Science 337:473-476(2012).
-!- FUNCTION: Sodium pump that utilizes the energy of pyrophosphate
hydrolysis as the driving force for Na(+) movement across the
membrane. {ECO:0000255|HAMAP-Rule:MF_01129,
ECO:0000269|PubMed:11343697, ECO:0000269|PubMed:17605473,
ECO:0000269|PubMed:22837527}.
-!- CATALYTIC ACTIVITY: Diphosphate + H(2)O = 2 phosphate.
{ECO:0000255|HAMAP-Rule:MF_01129, ECO:0000269|PubMed:15697234,
ECO:0000269|PubMed:17605473}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000255|HAMAP-Rule:MF_01129,
ECO:0000269|PubMed:11343697};
-!- ENZYME REGULATION: Inhibited by GdCl3. Requires K(+) for maximal
activity. K(+) greatly stimulates Na(+) binding. Thermostability
depends on the binding of Mg(2+). {ECO:0000269|PubMed:11343697,
ECO:0000269|PubMed:15697234, ECO:0000269|PubMed:22837527}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Temperature dependence:
Optimum temperature is 70 degrees Celsius.
{ECO:0000269|PubMed:11343697, ECO:0000269|PubMed:22837527};
-!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01129,
ECO:0000269|PubMed:16182234, ECO:0000269|PubMed:22837527}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-
Rule:MF_01129, ECO:0000269|PubMed:16182234}; Multi-pass membrane
protein {ECO:0000255|HAMAP-Rule:MF_01129,
ECO:0000269|PubMed:16182234}.
-!- DOMAIN: Has 16 transmembrane helices and a cytoplasmic domain that
contains the active site. Pyrophosphate binding is thought to
trigger a conformation change that allows Na(+) release. Has at
least two binding sites for Na(+) (PubMed:22837527).
{ECO:0000269|PubMed:22837527}.
-!- SIMILARITY: Belongs to the H(+)-translocating pyrophosphatase (TC
3.A.10) family. K(+)-stimulated subfamily. {ECO:0000255|HAMAP-
Rule:MF_01129}.
-----------------------------------------------------------------------
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EMBL; AE000512; AAD35267.1; -; Genomic_DNA.
EMBL; AF013268; AAC01564.2; -; Genomic_DNA.
PIR; D72409; D72409.
RefSeq; NP_227989.1; NC_000853.1.
RefSeq; WP_004082809.1; NZ_CP011107.1.
PDB; 4AV3; X-ray; 2.60 A; A/B=2-726.
PDB; 4AV6; X-ray; 4.00 A; A/B=2-726.
PDB; 5LZQ; X-ray; 3.50 A; A/B=2-726.
PDB; 5LZR; X-ray; 4.00 A; A/B=2-726.
PDBsum; 4AV3; -.
PDBsum; 4AV6; -.
PDBsum; 5LZQ; -.
PDBsum; 5LZR; -.
SMR; Q9S5X0; -.
DIP; DIP-61897N; -.
STRING; 243274.TM0174; -.
TCDB; 3.A.10.1.4; the h(+), na(+)-translocating pyrophosphatase (m(+)-ppase) family.
EnsemblBacteria; AAD35267; AAD35267; TM_0174.
GeneID; 897014; -.
KEGG; tma:TM0174; -.
eggNOG; ENOG4105EAY; Bacteria.
eggNOG; COG3808; LUCA.
InParanoid; Q9S5X0; -.
KO; K15987; -.
OMA; SIIAMFD; -.
BRENDA; 3.6.1.1; 6331.
Proteomes; UP000008183; Chromosome.
GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0009678; F:hydrogen-translocating pyrophosphatase activity; IEA:InterPro.
GO; GO:0004427; F:inorganic diphosphatase activity; IDA:UniProtKB.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0015081; F:sodium ion transmembrane transporter activity; IDA:UniProtKB.
GO; GO:0015992; P:proton transport; IEA:InterPro.
GO; GO:0035725; P:sodium ion transmembrane transport; IDA:UniProtKB.
HAMAP; MF_01129; PPase_energized_pump; 1.
InterPro; IPR004131; PPase-energised_H-pump.
PANTHER; PTHR31998; PTHR31998; 1.
Pfam; PF03030; H_PPase; 1.
PIRSF; PIRSF001265; H+-PPase; 1.
TIGRFAMs; TIGR01104; V_PPase; 1.
1: Evidence at protein level;
3D-structure; Calcium; Cell membrane; Complete proteome; Hydrolase;
Ion transport; Magnesium; Membrane; Metal-binding; Potassium;
Reference proteome; Sodium; Sodium transport; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 726 K(+)-stimulated pyrophosphate-energized
sodium pump.
/FTId=PRO_0000217005.
TOPO_DOM 1 1 Periplasmic.
{ECO:0000269|PubMed:22837527}.
TRANSMEM 2 22 Helical.
TOPO_DOM 23 46 Cytoplasmic.
{ECO:0000269|PubMed:22837527}.
TRANSMEM 47 71 Helical.
TOPO_DOM 72 73 Periplasmic.
{ECO:0000269|PubMed:22837527}.
TRANSMEM 74 97 Helical.
TOPO_DOM 98 122 Cytoplasmic.
{ECO:0000269|PubMed:22837527}.
TRANSMEM 123 153 Helical.
TOPO_DOM 154 168 Periplasmic.
{ECO:0000269|PubMed:22837527}.
TRANSMEM 169 197 Helical.
TOPO_DOM 198 235 Cytoplasmic.
{ECO:0000269|PubMed:22837527}.
TRANSMEM 236 261 Helical.
TOPO_DOM 262 284 Periplasmic.
{ECO:0000269|PubMed:22837527}.
TRANSMEM 285 309 Helical.
TOPO_DOM 310 320 Cytoplasmic.
{ECO:0000269|PubMed:22837527}.
TRANSMEM 321 343 Helical.
TOPO_DOM 344 358 Periplasmic.
{ECO:0000269|PubMed:22837527}.
TRANSMEM 359 379 Helical.
TOPO_DOM 380 405 Cytoplasmic.
{ECO:0000269|PubMed:22837527}.
TRANSMEM 406 430 Helical.
TOPO_DOM 431 436 Periplasmic.
{ECO:0000269|PubMed:22837527}.
TRANSMEM 437 463 Helical.
TOPO_DOM 464 492 Cytoplasmic.
{ECO:0000269|PubMed:22837527}.
TRANSMEM 493 520 Helical.
TOPO_DOM 521 541 Periplasmic.
{ECO:0000269|PubMed:22837527}.
TRANSMEM 542 571 Helical.
TOPO_DOM 572 601 Cytoplasmic.
{ECO:0000269|PubMed:22837527}.
TRANSMEM 602 629 Helical.
TOPO_DOM 630 630 Periplasmic.
{ECO:0000269|PubMed:22837527}.
TRANSMEM 631 658 Helical.
TOPO_DOM 659 697 Cytoplasmic.
{ECO:0000269|PubMed:22837527}.
TRANSMEM 698 722 Helical.
TOPO_DOM 723 726 Periplasmic.
{ECO:0000269|PubMed:22837527}.
METAL 202 202 Magnesium 1. {ECO:0000250}.
METAL 206 206 Magnesium 1. {ECO:0000250}.
METAL 229 229 Magnesium 2.
{ECO:0000269|PubMed:22837527}.
METAL 232 232 Magnesium 2.
{ECO:0000269|PubMed:22837527}.
METAL 465 465 Magnesium 2.
{ECO:0000269|PubMed:22837527}.
METAL 660 660 Calcium or magnesium.
{ECO:0000269|PubMed:22837527}.
METAL 688 688 Calcium or magnesium.
{ECO:0000269|PubMed:22837527}.
METAL 692 692 Calcium or magnesium.
{ECO:0000269|PubMed:22837527}.
BINDING 199 199 Substrate.
BINDING 695 695 Substrate.
SITE 191 191 Important for ion transport.
{ECO:0000250}.
SITE 236 236 Important for ion transport.
{ECO:0000250}.
SITE 243 243 Important for ion transport.
{ECO:0000250}.
SITE 495 495 Important for potassium dependence.
{ECO:0000305}.
SITE 696 696 Important for ion transport.
{ECO:0000250}.
SITE 707 707 Important for ion transport.
{ECO:0000250}.
MUTAGEN 190 190 D->A: No change in activity.
{ECO:0000269|PubMed:15697234}.
MUTAGEN 703 703 D->N: Silences the K(+)-independent
activating Na(+)-binding site.
{ECO:0000269|PubMed:15697234}.
HELIX 3 8 {ECO:0000244|PDB:4AV3}.
HELIX 10 26 {ECO:0000244|PDB:4AV3}.
HELIX 33 71 {ECO:0000244|PDB:4AV3}.
HELIX 74 108 {ECO:0000244|PDB:4AV3}.
TURN 109 112 {ECO:0000244|PDB:4AV3}.
HELIX 116 147 {ECO:0000244|PDB:4AV3}.
TURN 148 152 {ECO:0000244|PDB:4AV3}.
HELIX 154 157 {ECO:0000244|PDB:4AV3}.
HELIX 164 166 {ECO:0000244|PDB:5LZQ}.
HELIX 171 192 {ECO:0000244|PDB:4AV3}.
HELIX 194 205 {ECO:0000244|PDB:4AV3}.
HELIX 226 236 {ECO:0000244|PDB:4AV3}.
HELIX 238 265 {ECO:0000244|PDB:4AV3}.
STRAND 267 270 {ECO:0000244|PDB:4AV3}.
STRAND 273 278 {ECO:0000244|PDB:4AV3}.
HELIX 280 310 {ECO:0000244|PDB:4AV3}.
HELIX 317 344 {ECO:0000244|PDB:4AV3}.
HELIX 350 353 {ECO:0000244|PDB:4AV3}.
HELIX 358 360 {ECO:0000244|PDB:4AV3}.
HELIX 361 384 {ECO:0000244|PDB:4AV3}.
HELIX 389 397 {ECO:0000244|PDB:4AV3}.
HELIX 398 400 {ECO:0000244|PDB:4AV3}.
HELIX 402 416 {ECO:0000244|PDB:4AV3}.
HELIX 418 447 {ECO:0000244|PDB:4AV3}.
TURN 448 450 {ECO:0000244|PDB:4AV3}.
HELIX 451 474 {ECO:0000244|PDB:4AV3}.
HELIX 479 519 {ECO:0000244|PDB:4AV3}.
HELIX 524 526 {ECO:0000244|PDB:4AV3}.
STRAND 527 529 {ECO:0000244|PDB:4AV3}.
HELIX 531 533 {ECO:0000244|PDB:4AV3}.
HELIX 542 574 {ECO:0000244|PDB:4AV3}.
HELIX 577 583 {ECO:0000244|PDB:4AV3}.
TURN 584 587 {ECO:0000244|PDB:4AV3}.
HELIX 597 609 {ECO:0000244|PDB:4AV3}.
HELIX 612 629 {ECO:0000244|PDB:4AV3}.
HELIX 631 667 {ECO:0000244|PDB:4AV3}.
STRAND 671 673 {ECO:0000244|PDB:4AV3}.
STRAND 676 678 {ECO:0000244|PDB:4AV3}.
HELIX 679 696 {ECO:0000244|PDB:4AV3}.
HELIX 698 723 {ECO:0000244|PDB:4AV3}.
SEQUENCE 726 AA; 77046 MW; 492243F8C320BF93 CRC64;
MYVAALFFLI PLVALGFAAA NFAAVVRKPE GTERMKEISS YIRSGADSFL AHETKAIFKV
AIVIAILLMI FTTWQTGVAF LLGAVMSASA GIVGMKMATR ANVRVAEAAR TTKKIGPALK
VAYQGGSVMG LSVGGFALLG LVLVYLIFGK WMGQVDNLNI YTNWLGINFV PFAMTVSGYA
LGCSIIAMFD RVGGGVYTKA ADMAADLVGK TELNLPEDDP RNPATIADNV GDNVGDVAGL
GADLLESFVG AIVSSIILAS YMFPIYVQKI GENLVHQVPK ETIQALISYP IFFALVGLGC
SMLGILYVIV KKPSDNPQRE LNISLWTSAL LTVVLTAFLT YFYLKDLQGL DVVGFRFGAI
SPWFSAIIGI FSGILIGFWA EYYTSYRYKP TQFLSKSSIE GTGMVISNGL SLGMKSVFPP
TLTLVLGILF ADYFAGLYGV AIAALGMLSF VATSVSVDSY GPIADNAGGI SEMCELDPEV
RKITDHLDAV GNTTAAIGKG FAIGSAIFAA LSLFASYMFS QISPSDIGKP PSLVLLLNML
DARVIAGALL GAAITYYFSG YLISAVTKAA MKMVDEIRRQ AREIPGLLEG KAKPDYNRCI
EITSDNALKQ MGYPAFIAIL TPLVTGFLLG AEFVGGVLIG TVLSGAMLAI LTANSGGAWD
NAKKYLEAGN LEGYGKGSEP HKALVIGDTV GDPLKDTVGP SLDILIKIMS VVSVIAVSIF
KHVHLF


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