ID I3R344_HALMT Unreviewed; 892 AA.
AC I3R344;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Ca2+-transporting ATPase {ECO:0000313|EMBL:AFK18654.1};
DE EC=3.6.3.8 {ECO:0000313|EMBL:AFK18654.1};
GN Name=ctpA {ECO:0000313|EMBL:AFK18654.1};
GN OrderedLocusNames=HFX_0935 {ECO:0000313|EMBL:AFK18654.1};
OS Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC
OS 14739 / NCIMB 2177 / R-4) (Halobacterium mediterranei).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=523841 {ECO:0000313|EMBL:AFK18654.1, ECO:0000313|Proteomes:UP000006469};
RN [1] {ECO:0000313|EMBL:AFK18654.1, ECO:0000313|Proteomes:UP000006469}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 /
RC R-4 {ECO:0000313|Proteomes:UP000006469};
RX PubMed=22843593; DOI=10.1128/JB.00880-12;
RA Han J., Zhang F., Hou J., Liu X., Li M., Liu H., Cai L., Zhang B., Chen Y.,
RA Zhou J., Hu S., Xiang H.;
RT "Complete genome sequence of the metabolically versatile halophilic
RT archaeon Haloferax mediterranei, a poly(3-hydroxybutyrate-co-3-
RT hydroxyvalerate) producer.";
RL J. Bacteriol. 194:4463-4464(2012).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP001868; AFK18654.1; -; Genomic_DNA.
DR AlphaFoldDB; I3R344; -.
DR STRING; 523841.HFX_0935; -.
DR KEGG; hme:HFX_0935; -.
DR eggNOG; arCOG01578; Archaea.
DR HOGENOM; CLU_002360_4_1_2; -.
DR Proteomes; UP000006469; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR42861:SF29; SECRETORY PATHWAY CALCIUM ATPASE, ISOFORM G; 1.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00120; HATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000313|EMBL:AFK18654.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 55..76
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 250..268
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 274..302
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 683..709
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 715..742
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 763..790
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 796..813
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 833..858
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 864..885
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 2..75
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 892 AA; 94130 MW; 62496DF3C978E54C CRC64;
MPWHALESEA VLSNLDTSPD GLDSEEAAQR LDAYGPNILT EEDGISPLSL LVSQFTGPLI
LLLFVAAGLS LAVGVLPGRE PGYTDAVLIL LILLGNGLFG FIQDYRAEKA LAALREMSTP
DATVRRGGTV REISADEVVP GDIIILEAGD AVPADARILS AADCRADEST LTGESVPVGK
GPDPVDSDAA LADHRSVLHA GTTVVRGRAE AVVVATAMGT ELGTIADQLG QARQRETPFE
IEVDRLGRRI GIGIVALILV IAAIQLFVTA TDPVTVLLVA VTLAVAAVPE GLPAVVTLTL
ALGSRTLLNR NALVRNLSVV ESLGAVDFIV TDKTGTLTEN RMTVTRAWLP DDRTVELDDD
NGPELDPALS ALLSCGTRCN DAKKLDDGSY RGDPTEVALV SVAAEFGVDD DDKDGGGTGD
RLHEVSFTSE RKRMTIVVDE FDAPGDGPFA LMKGAPEVVL DRCDRVLVDG AIEPLGDELR
QRIETTTSEF ADDALRVLGF AYAPDADPNA DESALESELV FLGLQGMTDP PRDGVAGAVT
DCLNAGIHVT MATGDTPQTA RAIATEVGID ASSVLTGTEV GGLSDAELHR AIEETRVFAR
VSPEHKVRIL RALQDAGYTV AMTGDGVNDA PALGNADVGI AMGERGTQVA QGASDVVLRD
DNFVTIRDAI AEGRGIFDNI RKFVNYLLSA NTGEVLVVFL GTLLGALLFP EVFSASSALV
ITPVALLWIN LVTDGFPALA LGADPKSDDV MNRPPRPRHE GVLDRYTVAS IIGIGVALTG
TGLGVFFYAL SESGDLVVAQ TVLFTFLVTA ELVRTQSVRL RYRLSPFSNP WLLGAVGLSL
ALHLMLLYTP VSTLFGVVPL GLEAWGWIAG AFVPFLVANL LLVWVNDRVF DS
//
