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Database: UniProt
Entry: A0A0R2DLA1_9LACO
LinkDB: A0A0R2DLA1_9LACO
Original site: A0A0R2DLA1_9LACO 
ID   A0A0R2DLA1_9LACO        Unreviewed;       892 AA.
AC   A0A0R2DLA1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=P-type Ca(2+) transporter {ECO:0000256|ARBA:ARBA00012790};
DE            EC=7.2.2.10 {ECO:0000256|ARBA:ARBA00012790};
GN   ORFNames=FC86_GL000131 {ECO:0000313|EMBL:KRN04454.1};
OS   Holzapfeliella floricola DSM 23037 = JCM 16512.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Holzapfeliella.
OX   NCBI_TaxID=1423744 {ECO:0000313|EMBL:KRN04454.1, ECO:0000313|Proteomes:UP000051378};
RN   [1] {ECO:0000313|EMBL:KRN04454.1, ECO:0000313|Proteomes:UP000051378}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23037 {ECO:0000313|EMBL:KRN04454.1,
RC   ECO:0000313|Proteomes:UP000051378};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRN04454.1}.
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DR   EMBL; AYZL01000010; KRN04454.1; -; Genomic_DNA.
DR   RefSeq; WP_056974319.1; NZ_AYZL01000010.1.
DR   AlphaFoldDB; A0A0R2DLA1; -.
DR   STRING; 1423744.FC86_GL000131; -.
DR   PATRIC; fig|1423744.4.peg.135; -.
DR   OrthoDB; 9760364at2; -.
DR   Proteomes; UP000051378; Unassembled WGS sequence.
DR   GO; GO:0016020; C: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:0005388; F:P-type calcium transporter activity; IEA:UniProtKB-EC.
DR   CDD; cd02089; P-type_ATPase_Ca_prok; 1.
DR   Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR   Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR   Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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; IPR006408; P-type_ATPase_IIB.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01517; ATPase-IIB_Ca; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 3.
DR   PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR42861:SF156; CALCIUM-TRANSPORTING ATPASE; 1.
DR   Pfam; PF13246; Cation_ATPase; 1.
DR   Pfam; PF00689; Cation_ATPase_C; 1.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00120; HATPASE.
DR   SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SMART; SM00831; Cation_ATPase_N; 1.
DR   SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR   SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Calcium transport {ECO:0000256|ARBA:ARBA00022568};
KW   Ion transport {ECO:0000256|ARBA:ARBA00022568};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051378};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022568}.
FT   TRANSMEM        59..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        84..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        248..266
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        286..307
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        684..706
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        712..731
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        751..777
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        789..811
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        831..851
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        863..882
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          6..79
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
SQ   SEQUENCE   892 AA;  96579 MW;  D5F2D590ACF2352A CRC64;
     MENAKRIYAL TASEVEKKLN TSKEGLSSAE AKARLERDGL NTLQSKQSKS MLQKFFDQFK
     DFMIVVLLVA AVVSGVVAQE WADAIIILAV VLINAVLGVF QESKAEEAIE ALKEMSTPNA
     NVYRDGKMVS VPSDEVVLGD IVSVEAGDVI PADIRWLSTA SLQIEESALT GESVPVDKND
     KVLEDKDVPI GDRINLGFMN SNVTSGRGLG VVSAIGMQTE VGRIAGMLND TDETTTPLQE
     NLNSLGKVLT FLILIIAALI FVIGLFTNHE GLPLQTVATN MFLTAISLAV AAIPEGLPAI
     VTIILALGTQ KMAKRNALVR KLPAVETLGS TDIIASDKTG TLTMNQMTVE KVYYNGETHS
     AKDDIDANNS MLRVMNMAND TKIGGESELI GDPTETALVQ FGLNHKFNLD SVLKSEPRVE
     EVPFDSDRKL MSTIHKVQGN PYFVAVKGAP DELLKRVTKI ELNGKVTDIT EEQKQEILAT
     NTSMAKQALR VLAMAYKTVD QIPADPSTET VENDLVFAGL VGMIDPERPE AKQAIAEAKD
     AGITPIMITG DHQDTAEAIA GRLGIINPGD DSRVITGAQL DQMTPEEFKE RVPEFSVYAR
     VSPEHKVRIV KAWQSRGKVV AMTGDGVNDA PSLKTADIGI GMGITGTEVS KGASDMVLAD
     DNFATIVHAV REGRKVFSNI QKSIQYLLSA NLGEVLTLFF MTILGWDILK PVQLLWINLV
     TDTFPAIALG VEPSEPGVMK QKPRGRKSTF FSGGVSSAIF YQGVLEGALT LGVYLIGLHV
     GPHVNDYDML HADALTMAYV TLGLIQLFHA FNVKSVHQSL AQSNPFANKM LNLGILVSFV
     MLAVTIFVPG FNQLFHVTPL DLVQWAVVFA AGFAMIIIVE AVKFVQRRMG RQ
//
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