LLCA1_LACLA
ID LLCA1_LACLA Reviewed; 878 AA.
AC Q9CFU9;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Calcium-transporting ATPase 1;
DE EC=7.2.2.10;
DE AltName: Full=LLCA1;
GN Name=yoaB; OrderedLocusNames=LL1366; ORFNames=L2866;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND MUTAGENESIS OF
RP THR-54; MET-59 AND 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).
CC -!- FUNCTION: Catalyzes the hydrolysis of ATP coupled with the transport of
CC calcium. {ECO:0000269|PubMed:23621633}.
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:23621633};
CC -!- ACTIVITY REGULATION: Inhibited by very high concentrations of
CC cyclopiazonic acid (CPA). {ECO:0000269|PubMed:23621633}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
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; AE005176; AAK05464.1; -; Genomic_DNA.
DR PIR; F86795; F86795.
DR RefSeq; NP_267522.1; NC_002662.1.
DR RefSeq; WP_010905909.1; NC_002662.1.
DR AlphaFoldDB; Q9CFU9; -.
DR SMR; Q9CFU9; -.
DR STRING; 272623.L2866; -.
DR PaxDb; Q9CFU9; -.
DR EnsemblBacteria; AAK05464; AAK05464; L2866.
DR KEGG; lla:L2866; -.
DR PATRIC; fig|272623.7.peg.1472; -.
DR eggNOG; COG0474; Bacteria.
DR HOGENOM; CLU_002360_3_3_9; -.
DR OMA; RRFLTYH; -.
DR Proteomes; UP000002196; Chromosome.
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; 3.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Calcium; Calcium transport; Cell membrane; Ion transport;
KW Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..878
FT /note="Calcium-transporting ATPase 1"
FT /id="PRO_0000424526"
FT TRANSMEM 50..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 681..701
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 704..724
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 753..773
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 779..799
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 816..836
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 845..865
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 713
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 717
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 L-59 and P-295."
FT /evidence="ECO:0000269|PubMed:23621633"
FT MUTAGEN 59
FT /note="M->L: CPA-sensitive; when associated with Q-54 and
FT P-295."
FT /evidence="ECO:0000269|PubMed:23621633"
FT MUTAGEN 295
FT /note="S->P: Increases sensitivity to CPA. CPA-sensitive;
FT when associated with Q-54 and L-59."
FT /evidence="ECO:0000269|PubMed:23621633"
SQ SEQUENCE 878 AA; 96033 MW; 0D322BB263E3DF36 CRC64;
MQPYNQSVNE VLEETKSQFE GLSPKEVKNR QAKDGFNELK EKKKTSTWEL FIDTLKDPMV
IILLLVAFVQ LFLGEFVESL VIFIVLMINS VVAVVQTKRA ESSLDALRQM SAPSAKVLRN
GEKTSIPARE LVVGDIVSLE AGDFIPADGR LIDVQNLRVE EGMLTGESEP VEKFSDVIEG
EVALGDRKNM VFSSSLVVYG RADFLVTAIA EQTEIGKIAQ MLETAEAKQT PLQQKLEKFG
KQLGWVILAL CALIFAVQIL RLFTTNQTAD MQKAVLDSFM FAVAVAVAAI PEALSSVVTI
VLSVGTNKMA KQHAIMRNLP AVETLGSTSV ICTDKTGTLT QNKMTVVDSF LPTQGSKELT
DLTQADQKLL LNAMVLCNDS SFSQEGQLLG DPTEVALIAY SDKIGYPYQD LREKSPRLAE
FPFDSERKLM STINDFEGQK TIFVKGGPDV LFNRCNQVFL DGKVQEFTPE LKEKFQAQNE
AFSQKALRVL AYAYKPVSDN KTELTLTDEN DLILIGLSAM IDPPREAVYD SIAEAKKAGI
KTIMITGDHK TTAQAIAKDI GLMNEGDMAL TGQELDALTE DELRENLEKI SVYARVSPEN
KIRIVRAWQN EHQVTAMTGD GVNDAPALKQ ANIGIAMGSG TDVAKDASSM ILTDDNFVSI
VSAVSIGRVV YDNIKKSISY LFSGNLGAII AIVFALVVGW VNPFTALQLL FINLVNDSVP
AIALGMEKAE PDVMEKAPRQ LNEGIFANGL MRVILIRGSL IGIAAIISQY VGQKTSPEMG
VAMAFTTLIL ARTLQTFAAR SNSQNILKLG FTTNKYVLMA VTFCLALYSL TTLPFLREIF
SIPAAFGWSQ WIVAAGLAVI AVICMEILKS IKGVFEKH
