ATXB_LEIDO
ID ATXB_LEIDO Reviewed; 974 AA.
AC P12522;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=Probable proton ATPase 1B;
DE EC=7.1.2.1;
DE AltName: Full=LdH1B;
GN Name=H1B;
OS Leishmania donovani.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5661;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DEVELOPMENTAL STAGE.
RC STRAIN=MHOM/ET/67/L82;
RX PubMed=2469011; DOI=10.1016/0166-6851(89)90045-5;
RA Meade J.C., Hudson K.M., Stringer S.L., Stringer J.R.;
RT "A tandem pair of Leishmania donovani cation transporting ATPase genes
RT encode isoforms that are differentially expressed.";
RL Mol. Biochem. Parasitol. 33:81-91(1989).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H(+)(in) + H2O = ADP + 2 H(+)(out) + phosphate;
CC Xref=Rhea:RHEA:20852, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.1;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- DEVELOPMENTAL STAGE: More abundant in amastigotes than promastigotes.
CC {ECO:0000269|PubMed:2469011}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIIA subfamily. {ECO:0000305}.
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DR EMBL; AF109296; AAA29228.1; -; Genomic_DNA.
DR AlphaFoldDB; P12522; -.
DR SMR; P12522; -.
DR VEuPathDB; TriTrypDB:LdBPK_181510.1; -.
DR VEuPathDB; TriTrypDB:LdCL_180020400; -.
DR VEuPathDB; TriTrypDB:LDHU3_18.1900; -.
DR GO; GO:0016021; C:integral component of 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 GO; GO:0008553; F:P-type proton-exporting transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0120029; P:proton export across plasma membrane; IEA:InterPro.
DR CDD; cd02076; P-type_ATPase_H; 1.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
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; IPR006534; P-type_ATPase_IIIA.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR PRINTS; PR00120; HATPASE.
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; TIGR01647; ATPase-IIIA_H; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Hydrogen ion transport; Ion transport; Magnesium; Membrane;
KW Nucleotide-binding; Phosphoprotein; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..974
FT /note="Probable proton ATPase 1B"
FT /id="PRO_0000046181"
FT TRANSMEM 93..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..321
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 631..651
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 662..684
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 698..712
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 738..761
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 813..840
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 869..887
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 952..974
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 351
FT /note="4-aspartylphosphate intermediate"
SQ SEQUENCE 974 AA; 107305 MW; 9F58AB61186556B1 CRC64;
MSSKKYELDA AAFEDKPESH SDAEMTPQKP QRRQSVLSKA VSEHDERATG PATDLLPPSK
GLTTEEAEEL LKKYGRNELP EKKTPSWLIY VRGLWGPMPA ALWIAIIIEF ALENWPDGAI
LFAIQIANAT IGWYETIKAG DAVAALKNSL KPTATVYRDS KWQQIDAAVL VPGDLVKLAS
GSAVPADCSI NEGVIDVDEA ALTGESLPVT MGPEHMPKMG SNVVRGEVEG TVQYTGSLTF
FGKTAALLQS VESDLGNIHV ILRRVMLALC AISFILCMCC FIYLLARFYE TFRHALQFAV
VVLVVSIPIA LEIVVTTTLA VGSKHLSKHK IIVTKLSAIE MMSGVNMLCS DKTGTLTLNK
MEIQEQCFTF EEGNDLKSTL VLAALAAKWR EPPRDALDTM VLGAADLDEC DNYQQLNFVP
FDPTTKRTAA TLVDRRSGEK FDVTKGAPHV ILQMVYNQDE INDEVVDIID SLAARGVRCL
SVAKTDQQGR WHMAGILTFL DPPRPDTKDT IRRSKEYGVD VKMITGDHLL IAKEMCRMLD
LDPNILTADK LPQIKDANDL PEDLGEKYGD MMLSVGGFAQ VFPEHKFMIV ETLRQRGYTC
AMTGDGVNDA PALKRADVGI AVHGATDAAR AAADMVLTEP GLSVVVEAML VSREVFQRML
SFLTYRISAT LQLVCFFFIA CFSLTPKAYG SVDPNFQFFH LPVLMFMLIT LLNDGCLMTI
GYDHVIPSER PQKWNLPVVF VSASILAAVA CGSSLMLLWI GLEGYSSQYY ENSWFHRLGL
AQLPQGKLVT MMYLKISISD FLTLFSSRTG GHFFFYVPPS PILFCGAIIS LLVSTMAASF
WHKSRPDNVL TEGLAWGQTN AEKLLPLWVW IYCIVWWFVQ DVVKVLAHIC MDAVDLFGCV
SDASGSGPIK PYSDDMKVNG FEPVKKPAEK STEKALNLSV SSGPHKALEG LREDTHVLNE
STSPVNAFSP KVKK
