LMCA1_LISMO
ID LMCA1_LISMO Reviewed; 880 AA.
AC Q8Y8Q5;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Calcium-transporting ATPase lmo0841;
DE EC=7.2.2.10;
DE AltName: Full=LMCA1;
GN OrderedLocusNames=lmo0841;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
RN [2]
RP FUNCTION, STOICHIOMETRY, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP ALA-691 AND ARG-795.
RX PubMed=21047776; DOI=10.1074/jbc.m110.176784;
RA Faxen K., Andersen J.L., Gourdon P., Fedosova N., Morth J.P., Nissen P.,
RA Moller J.V.;
RT "Characterization of a Listeria monocytogenes Ca2+ Pump: a SERCA-type
RT ATPase with only one Ca2+-binding site.";
RL J. Biol. Chem. 286:1609-1617(2011).
RN [3]
RP ACTIVITY REGULATION, AND MUTAGENESIS OF THR-54; MET-59; SER-240 AND
RP SER-295.
RX PubMed=23621633; DOI=10.1111/febs.12310;
RA Kotsubei A., Gorgel M., Morth J.P., Nissen P., Andersen J.L.;
RT "Probing determinants of cyclopiazonic acid sensitivity of bacterial Ca2+-
RT ATPases.";
RL FEBS J. 280:5441-5449(2013).
RN [4]
RP CRYSTALLIZATION, AND SUBCELLULAR LOCATION.
RX PubMed=21636921; DOI=10.1107/s174430911101548x;
RA Andersen J.L., Gourdon P., Moller J.V., Morth J.P., Nissen P.;
RT "Crystallization and preliminary structural analysis of the Listeria
RT monocytogenes Ca(2+)-ATPase LMCA1.";
RL Acta Crystallogr. F 67:718-722(2011).
CC -!- FUNCTION: Catalyzes the hydrolysis of ATP coupled with the transport of
CC calcium. The transport is electrogenic with a probable ATP:Ca(2+):H(+)
CC stoichiometry of 1:1:1. May have an important role in survival of the
CC bacterium when stressed by a combination of a high calcium
CC concentration and alkaline pH. {ECO:0000269|PubMed:21047776}.
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:21047776};
CC -!- ACTIVITY REGULATION: Phosphorylation is inhibited by EGTA and vanadate.
CC ATPase activity is stimulated by Sr(2+). Inhibited by very high
CC concentrations of cyclopiazonic acid (CPA).
CC {ECO:0000269|PubMed:21047776, ECO:0000269|PubMed:23621633}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 9.0. {ECO:0000269|PubMed:21047776};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21047776,
CC ECO:0000269|PubMed:21636921}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:21047776, ECO:0000269|PubMed:21636921}.
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; AL591976; CAC98919.1; -; Genomic_DNA.
DR PIR; AI1179; AI1179.
DR RefSeq; NP_464367.1; NC_003210.1.
DR RefSeq; WP_003721406.1; NZ_CP023861.1.
DR PDB; 6ZHF; X-ray; 4.00 A; A=2-880.
DR PDB; 6ZHG; X-ray; 4.00 A; A=2-880.
DR PDB; 6ZHH; X-ray; 3.00 A; A/B/C/D/E/F/G/H=2-880.
DR PDBsum; 6ZHF; -.
DR PDBsum; 6ZHG; -.
DR PDBsum; 6ZHH; -.
DR AlphaFoldDB; Q8Y8Q5; -.
DR SMR; Q8Y8Q5; -.
DR STRING; 169963.lmo0841; -.
DR PaxDb; Q8Y8Q5; -.
DR EnsemblBacteria; CAC98919; CAC98919; CAC98919.
DR GeneID; 985338; -.
DR KEGG; lmo:lmo0841; -.
DR PATRIC; fig|169963.11.peg.864; -.
DR eggNOG; COG0474; Bacteria.
DR HOGENOM; CLU_002360_3_3_9; -.
DR OMA; RRFLTYH; -.
DR PhylomeDB; Q8Y8Q5; -.
DR BioCyc; LMON169963:LMO0841-MON; -.
DR Proteomes; UP000000817; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
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 GO; GO:0015662; F:P-type ion transporter activity; IBA:GO_Central.
DR GO; GO:0034220; P:ion transmembrane transport; 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; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Calcium; Calcium transport; Cell membrane;
KW Ion transport; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..880
FT /note="Calcium-transporting ATPase lmo0841"
FT /id="PRO_0000403478"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 681..701
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 707..727
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 756..776
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 819..839
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 854..874
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 334
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 287
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 288
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 290
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 292
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 716
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 720
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MUTAGEN 54
FT /note="T->Q: Increases sensitivity to CPA. CPA-sensitive;
FT when associated with P-295."
FT /evidence="ECO:0000269|PubMed:23621633"
FT MUTAGEN 59
FT /note="M->L: Does not affect sensitivity to CPA."
FT /evidence="ECO:0000269|PubMed:23621633"
FT MUTAGEN 240
FT /note="S->G: Does not affect sensitivity to CPA."
FT /evidence="ECO:0000269|PubMed:23621633"
FT MUTAGEN 295
FT /note="S->P: Strongly increases sensitivity to CPA. CPA-
FT sensitive; when associated with Q-54."
FT /evidence="ECO:0000269|PubMed:23621633"
FT MUTAGEN 691
FT /note="A->E: Displays optimal activity near pH 8.0."
FT /evidence="ECO:0000269|PubMed:21047776"
FT MUTAGEN 795
FT /note="R->E: Displays optimal activity near pH 8.0."
FT /evidence="ECO:0000269|PubMed:21047776"
FT MUTAGEN 795
FT /note="R->K: Shows very low activity, but no change in pH-
FT dependence."
FT /evidence="ECO:0000269|PubMed:21047776"
FT MUTAGEN 795
FT /note="R->Q: Displays optimal activity near pH 8.5."
FT /evidence="ECO:0000269|PubMed:21047776"
FT HELIX 8..15
FT /evidence="ECO:0007829|PDB:6ZHH"
FT HELIX 24..34
FT /evidence="ECO:0007829|PDB:6ZHH"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:6ZHH"
FT HELIX 53..56
FT /evidence="ECO:0007829|PDB:6ZHH"
FT HELIX 58..73
FT /evidence="ECO:0007829|PDB:6ZHH"
FT HELIX 76..99
FT /evidence="ECO:0007829|PDB:6ZHH"
FT HELIX 100..103
FT /evidence="ECO:0007829|PDB:6ZHH"
FT STRAND 113..119
FT /evidence="ECO:0007829|PDB:6ZHH"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:6ZHH"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:6ZHH"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:6ZHH"
FT STRAND 147..160
FT /evidence="ECO:0007829|PDB:6ZHH"
FT HELIX 162..165
FT /evidence="ECO:0007829|PDB:6ZHH"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:6ZHH"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:6ZHH"
FT STRAND 196..208
FT /evidence="ECO:0007829|PDB:6ZHH"
FT HELIX 214..224
FT /evidence="ECO:0007829|PDB:6ZHH"
FT HELIX 231..263
FT /evidence="ECO:0007829|PDB:6ZHH"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:6ZHH"
FT HELIX 271..289
FT /evidence="ECO:0007829|PDB:6ZHH"
FT HELIX 294..311
FT /evidence="ECO:0007829|PDB:6ZHH"
FT STRAND 314..318
FT /evidence="ECO:0007829|PDB:6ZHH"
FT HELIX 320..326
FT /evidence="ECO:0007829|PDB:6ZHH"
FT STRAND 330..333
FT /evidence="ECO:0007829|PDB:6ZHH"
FT HELIX 335..339
FT /evidence="ECO:0007829|PDB:6ZHH"
FT STRAND 345..350
FT /evidence="ECO:0007829|PDB:6ZHH"
FT HELIX 368..379
FT /evidence="ECO:0007829|PDB:6ZHH"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:6ZHH"
FT HELIX 395..406
FT /evidence="ECO:0007829|PDB:6ZHH"
FT HELIX 411..417
FT /evidence="ECO:0007829|PDB:6ZHH"
FT STRAND 422..424
FT /evidence="ECO:0007829|PDB:6ZHH"
FT STRAND 428..430
FT /evidence="ECO:0007829|PDB:6ZHH"
FT STRAND 433..439
FT /evidence="ECO:0007829|PDB:6ZHH"
FT STRAND 442..449
FT /evidence="ECO:0007829|PDB:6ZHH"
FT HELIX 451..455
FT /evidence="ECO:0007829|PDB:6ZHH"
FT STRAND 458..467
FT /evidence="ECO:0007829|PDB:6ZHH"
FT TURN 471..474
FT /evidence="ECO:0007829|PDB:6ZHH"
FT HELIX 475..487
FT /evidence="ECO:0007829|PDB:6ZHH"
FT STRAND 491..499
FT /evidence="ECO:0007829|PDB:6ZHH"
FT HELIX 509..511
FT /evidence="ECO:0007829|PDB:6ZHH"
FT STRAND 513..524
FT /evidence="ECO:0007829|PDB:6ZHH"
FT HELIX 531..540
FT /evidence="ECO:0007829|PDB:6ZHH"
FT STRAND 544..548
FT /evidence="ECO:0007829|PDB:6ZHH"
FT HELIX 553..561
FT /evidence="ECO:0007829|PDB:6ZHH"
FT TURN 562..564
FT /evidence="ECO:0007829|PDB:6ZHH"
FT HELIX 575..579
FT /evidence="ECO:0007829|PDB:6ZHH"
FT HELIX 583..589
FT /evidence="ECO:0007829|PDB:6ZHH"
FT HELIX 590..592
FT /evidence="ECO:0007829|PDB:6ZHH"
FT STRAND 595..598
FT /evidence="ECO:0007829|PDB:6ZHH"
FT HELIX 601..613
FT /evidence="ECO:0007829|PDB:6ZHH"
FT STRAND 618..622
FT /evidence="ECO:0007829|PDB:6ZHH"
FT HELIX 625..627
FT /evidence="ECO:0007829|PDB:6ZHH"
FT HELIX 628..633
FT /evidence="ECO:0007829|PDB:6ZHH"
FT STRAND 634..640
FT /evidence="ECO:0007829|PDB:6ZHH"
FT HELIX 645..650
FT /evidence="ECO:0007829|PDB:6ZHH"
FT STRAND 652..655
FT /evidence="ECO:0007829|PDB:6ZHH"
FT HELIX 662..700
FT /evidence="ECO:0007829|PDB:6ZHH"
FT HELIX 709..717
FT /evidence="ECO:0007829|PDB:6ZHH"
FT TURN 718..720
FT /evidence="ECO:0007829|PDB:6ZHH"
FT HELIX 721..728
FT /evidence="ECO:0007829|PDB:6ZHH"
FT TURN 734..737
FT /evidence="ECO:0007829|PDB:6ZHH"
FT TURN 748..752
FT /evidence="ECO:0007829|PDB:6ZHH"
FT HELIX 753..776
FT /evidence="ECO:0007829|PDB:6ZHH"
FT HELIX 780..802
FT /evidence="ECO:0007829|PDB:6ZHH"
FT STRAND 805..807
FT /evidence="ECO:0007829|PDB:6ZHH"
FT HELIX 809..812
FT /evidence="ECO:0007829|PDB:6ZHH"
FT TURN 814..816
FT /evidence="ECO:0007829|PDB:6ZHH"
FT HELIX 818..834
FT /evidence="ECO:0007829|PDB:6ZHH"
FT TURN 837..844
FT /evidence="ECO:0007829|PDB:6ZHH"
FT HELIX 851..878
FT /evidence="ECO:0007829|PDB:6ZHH"
SQ SEQUENCE 880 AA; 95658 MW; ED088BDD461D29B1 CRC64;
MEIYRKSAAE TFTQLEATEK GLTTSEVTKR QEKYGFNELK NKKKDPLWKL FLETFKDPMV
IVLVIAALVQ LVLGEVVESL IIFLVLIVNS IISVVQTRKA ESSLDALREM SAPVAKVIRD
GSKQSIHARE LVPGDVVILD AGDFVPADGR LFESGSLKID EGMLTGESEA VEKYIDTIPD
EVGLGDRVNM VFSGSLVVYG RGMFVVTGTA SETEIGKIAG LLETAEAKQT PLQRKLESFS
KKLGLGILAL CVLIFAVEAG RVLLGDNSAD MATAILNAFM FAVAVAVAAI PEALSSIVTI
VLAVGTNKMA KQHAIIRKLP AVETLGSTSV ICTDKTGTLT QNKMTVVDYY LPDGTKENFP
ESPENWSEGE RRLIHIAVLC NDSNINSEGK ELGDPTEVAL IAFSNKNNQD YNEIREKFIR
EGEIPFDSDR KLMSTLHTFN ENKAMLTKGG PDVMFARCSY VFLDGEEKPM TEEILAKLKE
TNEEFSNQAL RVLAYGYKRM PADTTELKLE DEQDIVLVGL TAMIDPPREA VYASIEESKK
AGIRTVMITG DHKTTAQAIG RDIGLMDADD IALTGQELDA MPEEELDKKL EHIAVYARVS
PENKIRIVKA WQKKGKITAM TGDGVNDAPA LKQADIGVAM GSGTDVAKDS AAMILTDDNF
VSIVDAVGVG RTVFDNIKKS IAYLFAGNLG AIIAILFALV LDWINPFTAL QLLFINLVND
SLPAIALGME KAEPDVMKRK PRDINEGIFA GGTMRAVISR GVLIGIAVII SQYIGMQISP
EMSVAMAFTT LILARTLQTF AARSNVQTAF GAGFFSNKYV IGAVLLCFVL YGITVLPGAR
EIFSIPASFG LHEWSIAAGL ALAAVVMMEI IKVVQNKFFK
