ID M1Q9Q5_BACTU Unreviewed; 888 AA.
AC M1Q9Q5;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Cation-transporting ATPase, E1-E2 family {ECO:0000313|EMBL:AGF99105.1};
GN ORFNames=H175_ch0392 {ECO:0000313|EMBL:AGF99105.1};
OS Bacillus thuringiensis serovar thuringiensis str. IS5056.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1286404 {ECO:0000313|EMBL:AGF99105.1, ECO:0000313|Proteomes:UP000011719};
RN [1] {ECO:0000313|EMBL:AGF99105.1, ECO:0000313|Proteomes:UP000011719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IS5056 {ECO:0000313|EMBL:AGF99105.1};
RX PubMed=23516221;
RA Murawska E., Fiedoruk K., Bideshi D.K., Swiecicka I.;
RT "Complete genome sequence of Bacillus thuringiensis subsp. thuringiensis
RT strain IS5056, an isolate highly toxic to Trichoplusia ni.";
RL Genome Announc. 1:E0010813-E0010813(2013).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP004123; AGF99105.1; -; Genomic_DNA.
DR RefSeq; WP_000073697.1; NC_020376.1.
DR AlphaFoldDB; M1Q9Q5; -.
DR SMR; M1Q9Q5; -.
DR GeneID; 67464995; -.
DR KEGG; btht:H175_ch0392; -.
DR PATRIC; fig|1286404.3.peg.404; -.
DR HOGENOM; CLU_002360_1_1_9; -.
DR Proteomes; UP000011719; Chromosome.
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:0006811; P:monoatomic ion transport; IEA:UniProtKB-KW.
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; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01494; ATPase_P-type; 4.
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; PR00121; NAKATPASE.
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 Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
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:ARBA00022448}.
FT TRANSMEM 53..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 81..97
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 249..267
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 279..303
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 675..698
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 743..770
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 830..852
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 864..882
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 3..77
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 888 AA; 97666 MW; C12FEE278AA0A0A7 CRC64;
MSNWYSKTKD QTLIDLETNE QHGLTDEIVS ERLKQYGSNE LATKQKRTLW QRIFAQINDV
LVYVLIIAAL ISAFVGEWAD ASIIALVVVL NAVIGVVQES KAEQALEALK KMATPKAIVK
RNGELKEIPS EHVVPGDIVM LDAGRYIPCD LRLIETANLK VEESALTGES VPVDKDAIYH
PSMQSDEQVP LGDQKNMAFM STLVTYGRGV GVAVETGMNS QIGKIATLLH EADDDMTPLQ
KSLAQVGKYL GFVAVAICIV MFLIGFLQGR DTLEMFMTAI SLAVAAIPEG LPAIVSIVLA
IGVQRMIKQN VIIRKLPAVE ALGSVTIICS DKTGTLTQNK MTVTHFYSDN TYDRLESLNV
NNDAQRLLLE NMVLCNDASY TNESQTGDPT EIALLVAGTT FNMQKDHLEK IHERVNEVPF
DSDRKMMSTV HTYDESYYSM TKGAIDKLLP RCTHIFKNGK IEILTDSDKN QILEAAGAMS
QEALRVLSFA FKQYNSNDVD INHLEENLIF IGLVGMIDPP RTEVKDSITE CKKAGIRTVM
ITGDHKDTAF AIAKELGIAE EISEIMIGTE LDNISDTELA SKINHLNVFA RVSPEHKVKI
VKALRAKGNI VSMTGDGVND APSLKQADVG VAMGITGTDV AKGAADVVLT DDNFSSIVKA
VEEGRNIYRN IKKSILFLLS CNFGEIIALF LAILLGWATP LRPIHILWVN LITDTLPALS
LGVDPEDPDV MKEKPRHAKE SLFSGSVPFL IFNGVIIGLL TLIAFIAGAK FYTGDTNLFP
LFPERIDDDA LLHAQTMAFV VLSFSQLVHS FNLRSRTKSI FSIGIFTNKY LVFSLLIGVL
MQVCIISIPP LANIFGVHAL TMRDWGFVLL LSIIPLIVNE IIKLVKRN
//