ATCL_SYNE7
ID ATCL_SYNE7 Reviewed; 926 AA.
AC P37278; Q31PA7;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Calcium-transporting ATPase;
DE EC=7.2.2.10;
DE AltName: Full=Calcium pump;
GN Name=pacL; OrderedLocusNames=Synpcc7942_1082;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=8370468; DOI=10.1016/0014-5793(93)80928-n;
RA Kanamaru K., Kashiwagi S., Mizuno T.;
RT "The cyanobacterium, Synechococcus sp. PCC7942, possesses two distinct
RT genes encoding cation-transporting P-type ATPases.";
RL FEBS Lett. 330:99-104(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION,
RP AND DISRUPTION PHENOTYPE.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=8021228; DOI=10.1128/jb.176.14.4430-4436.1994;
RA Berkelman T., Garret-Engele P., Hoffman N.E.;
RT "The pacL gene of Synechococcus sp. strain PCC 7942 encodes a Ca(2+)-
RT transporting ATPase.";
RL J. Bacteriol. 176:4430-4436(1994).
CC -!- FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of
CC ATP coupled with the transport of calcium. In vivo, probably exports
CC the calcium from the cytoplasm to the periplasm and the extracellular
CC medium. {ECO:0000269|PubMed:8021228}.
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 Evidence={ECO:0000269|PubMed:8021228};
CC -!- ACTIVITY REGULATION: Inhibited by vanadate.
CC {ECO:0000269|PubMed:8021228}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:8021228};
CC Multi-pass membrane protein {ECO:0000269|PubMed:8021228}.
CC -!- DISRUPTION PHENOTYPE: Hypersensitive to osmotic stress. Mutant lacks
CC ATP-dependent calcium transport. {ECO:0000269|PubMed:8021228,
CC ECO:0000269|PubMed:8370468}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIA subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABB57112.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D16436; BAA03906.1; -; Genomic_DNA.
DR EMBL; CP000100; ABB57112.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_049749327.1; NC_007604.1.
DR AlphaFoldDB; P37278; -.
DR SMR; P37278; -.
DR STRING; 1140.Synpcc7942_1082; -.
DR PRIDE; P37278; -.
DR EnsemblBacteria; ABB57112; ABB57112; Synpcc7942_1082.
DR KEGG; syf:Synpcc7942_1082; -.
DR eggNOG; COG0474; Bacteria.
DR HOGENOM; CLU_002360_3_3_3; -.
DR OrthoDB; 178322at2; -.
DR BioCyc; SYNEL:SYNPCC7942_1082-MON; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 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; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Calcium; Calcium transport; Cell inner membrane;
KW Cell membrane; Ion transport; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..926
FT /note="Calcium-transporting ATPase"
FT /id="PRO_0000046159"
FT TOPO_DOM 1..63
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 85..99
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 121..259
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..279
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 280..291
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 310..716
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 717..736
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 737..747
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 748..768
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 769..788
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 789..811
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 812..832
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 833..852
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 853..864
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 865..883
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 884..898
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 899..919
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 920..926
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 347
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 300
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 301
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 305
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 661
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 665
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 727
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 730
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 756
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 759
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 760
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 760
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CONFLICT 923..924
FT /note="QR -> HG (in Ref. 1; BAA03906)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 926 AA; 99787 MW; 38A6BACF7370A1B6 CRC64;
MKGAIVSASL TDVRQPIAHW HSLTVEECHQ QLDAHRNGLT AEVAADRLAL YGPNELVEQA
GRSPLQILWD QFANIMLLML LAVAVVSGAL DLRDGQFPKD AIAILVIVVL NAVLGYLQES
RAEKALAALK GMAAPLVRVR RDNRDQEIPV AGLVPGDLIL LEAGDQVPAD ARLVESANLQ
VKESALTGEA EAVQKLADQQ LPTDVVIGDR TNCLFQGTEV LQGRGQALVY ATGMNTELGR
IATLLQSVES EKTPLQQRLD KLGNVLVSGA LILVAIVVGL GVLNGQSWED LLSVGLSMAV
AIVPEGLPAV ITVALAIGTQ RMVQRESLIR RLPAVETLGS VTTICSDKTG TLTQNKMVVQ
QIHTLDHDFT VTGEGYVPAG HFLIGGEIIV PNDYRDLMLL LAAGAVCNDA ALVASGEHWS
IVGDPTEGSL LTVAAKAGID PEGLQRVLPR QDEIPFTSER KRMSVVVADL GETTLTIREG
QPYVLFVKGS AELILERCQH CFGNAQLESL TAATRQQILA AGEAMASAGM RVLGFAYRPS
AIADVDEDAE TDLTWLGLMG QIDAPRPEVR EAVQRCRQAG IRTLMITGDH PLTAQAIARD
LGITEVGHPV LTGQQLSAMN GAELDAAVRS VEVYARVAPE HKLRIVESLQ RQGEFVAMTG
DGVNDAPALK QANIGVAMGI TGTDVSKEAS DMVLLDDNFA TIVAAVEEGR IVYGNIRKFI
KYILGSNIGE LLTIASAPLL GLGAVPLTPL QILWMNLVTD GIPALALAVE PGDPTIMQRR
PHNPQESIFA RGLGTYMLRV GVVFSAFTIV LMVIAYQYTQ VPLPGLDPKR WQTMVFTTLC
LAQMGHAIAV RSDLLTIQTP MRTNPWLWLS VIVTALLQLA LVYVSPLQKF FGTHSLSQLD
LAICLGFSLL LFVYLEAEKW VRQRRY
