ATA1_SYNY3
ID ATA1_SYNY3 Reviewed; 905 AA.
AC P37367; P73840;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 25-MAY-2022, entry version 157.
DE RecName: Full=Cation-transporting ATPase pma1;
DE EC=7.2.2.-;
GN Name=pma1; OrderedLocusNames=sll1614;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8263933; DOI=10.1006/jmbi.1993.1684;
RA Geisler M., Richter J., Schumann J.;
RT "Molecular cloning of a P-type ATPase gene from the cyanobacterium
RT Synechocystis sp. PCC 6803. Homology to eukaryotic Ca(2+)-ATPases.";
RL J. Mol. Biol. 234:1284-1289(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
CC -!- FUNCTION: Could mediate calcium influx.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIA subfamily. {ECO:0000305}.
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DR EMBL; X71022; CAA50340.1; -; Genomic_DNA.
DR EMBL; BA000022; BAA17897.1; -; Genomic_DNA.
DR PIR; S75035; S75035.
DR AlphaFoldDB; P37367; -.
DR SMR; P37367; -.
DR IntAct; P37367; 51.
DR STRING; 1148.1652980; -.
DR TCDB; 3.A.3.2.4; the p-type atpase (p-atpase) superfamily.
DR PaxDb; P37367; -.
DR EnsemblBacteria; BAA17897; BAA17897; BAA17897.
DR KEGG; syn:sll1614; -.
DR eggNOG; COG0474; Bacteria.
DR InParanoid; P37367; -.
DR OMA; PLWNNMM; -.
DR PhylomeDB; P37367; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled cation transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005388; F:P-type calcium transporter activity; IBA:GO_Central.
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; 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 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; TIGR01494; ATPase_P-type; 3.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Magnesium; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..905
FT /note="Cation-transporting ATPase pma1"
FT /id="PRO_0000046178"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 716..736
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 774..794
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 809..829
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 848..868
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 880..900
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 333
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000305"
FT CONFLICT 1..34
FT /note="MDFPTLSSYLHHHRPGEDILADLHTDPGLGLTAE -> MGAFPLPPNQYGFP
FT HLKFLPPSPSTRGRHSCRFAHRSRFRSDSG (in Ref. 1; CAA50340)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="A -> G (in Ref. 1; CAA50340)"
FT /evidence="ECO:0000305"
FT CONFLICT 897
FT /note="A -> R (in Ref. 1; CAA50340)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 905 AA; 97590 MW; 0E438F17DE581D61 CRC64;
MDFPTLSSYL HHHRPGEDIL ADLHTDPGLG LTAEAVAQRY EQYGRNELKF KPGKPAWLRF
LLQFHQPLLY ILLIAGTVKA FLGSWTNAWV IWGVTLVNAI IGYIQEAKAE GAIASLAKAV
TTEATVLRDG QNLRIPSQDL VIGDIVSLAS GDKVPADLRL LKVRNLQVDE SALTGEAVPV
EKAVELLPEE TPLAERLNMA YAGSFVTFGQ GTGVVVATAN ATEMGQISQS MEKQVSLMTP
LTRKFAKFSH TLLYVIVTLA AFTFAVGWGR GGSPLEMFEA AVALAVSAIP EGLPAVVTVT
LAIGVNRMAK RNAIIRKLPA VEALGSATVV CSDKTGTLTE NQMTVQAVYA GGKHYEVSGG
GYSPKGEFWQ VMGEEVDNVL LDGLPPVLEE CLLTGMLCND SQLEHRGDDW AVVGDPTEGA
LLASAAKAGF SQAGLASQKP RLDSIPFESD YQYMATLHDG DGRTIYVKGS VESLLQRCES
MLLDDGQMVS IDRGEIEENV EDMAQQGLRV LAFAKKTVEP HHHAIDHGDI ETGLIFLGLQ
GMIDPPRPEA IAAVHACHDA GIEVKMITGD HISTAQAIAK RMGIAAEGDG IAFEGRQLAT
MGPAELAQAA EDSCVFARVA PAQKLQLVEA LQEKGHIVAM TGDGVNDAPA LKRADIGIAM
GKGGTEVARE SSDMLLTDDN FASIEAAVEE GRTVYQNLRK AIAFLLPVNG GESMTILISV
LLALNLPILS LQVLWLNMIN SITMTVPLAF EAKSPGIMQQ APRNPNEPLI TKKLLHRILL
VSLFNWILIF GMFEWVNRTY DDLALARTMA IQALVAARVI YLLSISQLGR SFLGYVTGKR
QTITKASILL LGIAVAIALQ IGFSQLPFMN VLFKTAPMDW QQWAICLLPM IPMVPVAILA
NRLDP
