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Database: UniProt
Entry: D6Y2R7_THEBD
LinkDB: D6Y2R7_THEBD
Original site: D6Y2R7_THEBD 
ID   D6Y2R7_THEBD            Unreviewed;      1461 AA.
AC   D6Y2R7;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   SubName: Full=ATPase, P-type (Transporting), HAD superfamily, subfamily IC {ECO:0000313|EMBL:ADG86878.1};
DE            EC=3.6.3.8 {ECO:0000313|EMBL:ADG86878.1};
GN   OrderedLocusNames=Tbis_0146 {ECO:0000313|EMBL:ADG86878.1};
OS   Thermobispora bispora (strain ATCC 19993 / DSM 43833 / CBS 139.67 / JCM
OS   10125 / KCTC 9307 / NBRC 14880 / R51).
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Thermobispora.
OX   NCBI_TaxID=469371 {ECO:0000313|EMBL:ADG86878.1, ECO:0000313|Proteomes:UP000006640};
RN   [1] {ECO:0000313|EMBL:ADG86878.1, ECO:0000313|Proteomes:UP000006640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19993 / DSM 43833 / CBS 139.67 / JCM 10125 / KCTC 9307 /
RC   NBRC 14880 / R51 {ECO:0000313|Proteomes:UP000006640};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Mikhailova N., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F.,
RA   Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T.,
RA   Wu D., Jando M., Schneider S., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Thermobispora bispora DSM 43833.";
RL   Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
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         Evidence={ECO:0000256|ARBA:ARBA00001836};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CP001874; ADG86878.1; -; Genomic_DNA.
DR   RefSeq; WP_013130411.1; NC_014165.1.
DR   STRING; 469371.Tbis_0146; -.
DR   KEGG; tbi:Tbis_0146; -.
DR   eggNOG; COG0474; Bacteria.
DR   eggNOG; COG2217; Bacteria.
DR   HOGENOM; CLU_002360_0_1_11; -.
DR   OrthoDB; 9814270at2; -.
DR   Proteomes; UP000006640; Chromosome.
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   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; 2.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
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   NCBIfam; TIGR01494; ATPase_P-type; 2.
DR   PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR42861:SF29; SECRETORY PATHWAY CALCIUM ATPASE, ISOFORM G; 1.
DR   Pfam; PF00689; Cation_ATPase_C; 1.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00120; HATPASE.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 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   Hydrolase {ECO:0000313|EMBL:ADG86878.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006640};
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}.
FT   TRANSMEM        1333..1351
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1386..1406
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1418..1437
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          601..672
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
SQ   SEQUENCE   1461 AA;  154609 MW;  379D2550266DEF30 CRC64;
     MFLTQLFASY APVLRDVLPE PLRGLVVTPR RVIACPGGLR IDLRGIGGPG TERSAALLEE
     RLSALPGVER AEVNGRLGCV FVGCDPEAVD REELLEIARE LDEQERHAHE TPVRVVEEHI
     RSIIRLATGV AGVGTIFTGI ALRAPRLSPA VPALVNLLNA TPVLREELDK RIGRGPANAL
     FHTANLVTQT LTLRPLGLVA HSMAALSRYV ETRAAQRSWV ALERRLAEVP GSYRHVRARF
     RRRPTHLPHG PIERYADLAS TAAALTYGFM RFAARQDERA LAVLTAITPK IAEYTREAFA
     GAVRRALGER DTVVFDAEAL RRMDRVDTVV LDSDALTTGS WAIDRVEPLV DELDLNELYA
     RLYRLLDFTD PGATRIDEEW SAAPLTDPAR FPGTHATEWR GRGMRLVEVR RADTPVALVG
     LSREIDPLAV PIVAAAKAAG TVLLAGDEDG TAHRLAIDQV LPGGADLAHR VFEMQAEGHC
     VLVVSRRARE ALAQADIGFG VMDPGTATVP WDADVAGGLP GLHLLLIGLR RAETASRDGV
     RIGVAGGLIG ALFSFAGPAS GAVGRAQLVS SLGALVAVAW GELAGRALAR TPVPLRADPT
     PWHAMSVPEV LARLGSSPRG ISEEEAERRR AAARPVEIAA PRSLARTVLG ELANPLTPAL
     ASGAAIAALI GSAVDSVMIS GVMVINAFIG GVQQSQADRE LTRLTETTSV RVRVRRPEGT
     VEIRKEDLVP GDVVELRAGD AIPADGRVIK SVGLEVDEST LTGESQLIAK RTEPTIAAAI
     ADRASMVYEG TTVAAGTGLA VVVATGEMTE ARRAAQLGTA PPRVSGVELR MRELSRRVLP
     LSVGSGLFLL VTELLRGRSL AAALVPAVSL TVAAVPEGLP FVATAAELAA ARRLSRRAAL
     VRNPKTIEAL GRVNVLCFDK TGTLTEGRIS LQYVSDGRAG RPVEELTHHL RRVIAAAVRA
     SPKTGGGRVL AHPTDRAIHE AAERLSITPR EGLQVWERVD EMPFEPGRGY HAVLGRTEHG
     HLLSVKGAPE IVIDHCTTAL RGTEVVPCDD AVRHELTREV ARLARQGYRV LAVAQRPASD
     RSDLDESRID ELCFLGFLGL ADPVRATAAE SVDRLMRAGV RIVMITGDHP STAEAIAVEL
     NTLNGGRIMT GPELDELDDE TLTKLLPEVS VFARVTPAHK VRIVSCLRRA GEVVAVTGDG
     ANDAPAIRIA NVGIALGSRA TPAARSAADL VVTDDRIETV VDAIVEGRAM WSSVRDALSI
     LVGGNLGEII YTIASSLIGA TALNARQLLL VNLLTDLAPA IAVALRPPTS TEPERLLTEG
     PEASLGASLM REIYVRAGVT ALAAAMGWLA GRATGTRGRA ATIGLVALVT AQLLQTLSGG
     GTNRTVVLAV LASFALLCVI VTAPGVSGFF GCRPLGPVGW TVGLGSAGLA ALIGEVVQRW
     LLRPVASAAP RPALTPAPAA A
//
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