ATC_TRYBB
ID ATC_TRYBB Reviewed; 1011 AA.
AC P35315;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Probable calcium-transporting ATPase;
DE EC=7.2.2.10;
DE AltName: Full=Calcium pump;
GN Name=TBA1;
OS Trypanosoma brucei brucei.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=5702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1833643; DOI=10.1016/0166-6851(91)90048-b;
RA Revelard P., Pays E.;
RT "Structure and transcription of a P-ATPase gene from Trypanosoma brucei.";
RL Mol. Biochem. Parasitol. 46:241-251(1991).
CC -!- FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of
CC ATP coupled with the transport of the calcium. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; EC=7.2.2.10;
CC -!- SUBCELLULAR LOCATION: Flagellar pocket. Cell membrane; Multi-pass
CC membrane protein. Note=May be located in the flagellar pocket of the
CC membrane.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. {ECO:0000305}.
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DR EMBL; M73769; AAA30227.1; -; Genomic_DNA.
DR AlphaFoldDB; P35315; -.
DR SMR; P35315; -.
DR PRIDE; P35315; -.
DR GO; GO:0020016; C:ciliary pocket; IEA:UniProtKB-SubCell.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0005388; F:P-type calcium transporter activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 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; IPR005782; P-type_ATPase_IIA.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01116; ATPase-IIA1_Ca; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Calcium; Calcium transport; Cell membrane; Ion transport;
KW Magnesium; Membrane; Nucleotide-binding; Phosphoprotein; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1011
FT /note="Probable calcium-transporting ATPase"
FT /id="PRO_0000046228"
FT TOPO_DOM 1..65
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 85..90
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111..258
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 259..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 279..303
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..321
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 322..770
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 771..794
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 795..835
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 836..856
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 857..885
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 886..905
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 906..922
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 923..942
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 943..1011
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 357
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 514
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1011 AA; 110314 MW; 4F2103FED2A7D5D0 CRC64;
MLPENLPTDP AAMTPAAVAA ALRVDTKVGL SSNEVEERRQ AFGINELPSE PPTPFWKLVL
AQFEDTLVRI LLLAATVSFA MAVVENNAAD FVEPFIILLI LILNATVGVW QENRAEGAIE
ALKSFVPKTA VVLRDGDIKT VNAEELVPGD VVEVAVGNRV PADMRVVELH STTLRADQSI
LNGESVEAMK QIEAVKGRQE RFPACMVYSG TAIVYGKALC VVVRTGASTE IGTIERDVRE
QEEVKTPLQV KLDEFGVLLS KVIGYICLVV FAVNLVRWYA THKPTKNETF FTRYIQPSVH
CLKVAVALAV AAIPEGLPAV VTTCLALGTR RMAQHNALVR DLPSVETLGR CTVICSDKTG
TLTTNMMSVL HAFTLKGDGS IKEYELKDSR FNIVSNSVTC EGRQVSSPLE QDGALTKLAN
IAVLCNDASL HHNAATVQVE KIGEATEAAL LVMSEKFANI KGDSAVNAFR TLCEGKWKKN
ATLEFTRKRK SMSVHVTSTV TGSPASSTNN LFVKGAPEEV LRRSTHVMQD NGAVVQLSAT
HRKRIIEQLD KISGGANALR CIGFAFKPTK AVQHVRLNDP ATFEDVESDL TFVGACGMLD
PPREEVRDAI VKCRTAGIRV VVITGDRKET AEAICCKLGL LSSTADTTGL SYTGQELDAM
TPAQKREAVL TAVLFSRTDP SHKMQLVQLL KDERLICAMT GDGVNDAPAL KKADIGIAMG
SGTEVAKSAS KMVLADDNFA TVVKAVQEGR AIYNNTKQFI RYLISSNIGE VVCILVTGLF
GLPEALSPVQ LLWVNLVTDG LPATALGFNA PDRDIMEQRP RRMEEPIVNG WLFMRYMVIG
VYVGLATVGG FLWWFLRHGF SWHDLTTYTA CSDMTNGTCL LLANPQTARA IALSILVVVE
MLNALNALSE NASLIVSRPS SNVWLLFAIF SSLSLHLIIM YVPFFAKLFN IVPLGVDPHV
VQQAQPWSIL TPTNFDDWKA VIVFSVPVIF LDELLKFITR RMEKAQEKKK D
