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Database: UniProt
Entry: A0A345T4H7_9ACTN
LinkDB: A0A345T4H7_9ACTN
Original site: A0A345T4H7_9ACTN 
ID   A0A345T4H7_9ACTN        Unreviewed;      1586 AA.
AC   A0A345T4H7;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Cation-translocating P-type ATPase {ECO:0000313|EMBL:AXI80882.1};
GN   ORFNames=C7M71_029385 {ECO:0000313|EMBL:AXI80882.1};
OS   Peterkaempfera bronchialis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Peterkaempfera.
OX   NCBI_TaxID=2126346 {ECO:0000313|EMBL:AXI80882.1, ECO:0000313|Proteomes:UP000249340};
RN   [1] {ECO:0000313|Proteomes:UP000249340}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 106435 {ECO:0000313|Proteomes:UP000249340};
RA   Batra D., Gulvik C.A.;
RT   "Streptacidiphilus bronchialis DSM 106435 chromosome.";
RL   Submitted (JUL-2018) 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; CP031264; AXI80882.1; -; Genomic_DNA.
DR   KEGG; stri:C7M71_029385; -.
DR   OrthoDB; 9814270at2; -.
DR   Proteomes; UP000249340; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
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; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 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   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   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000249340};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          1414..1569
FT                   /note="Cation-transporting P-type ATPase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00689"
FT   REGION          304..324
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          697..726
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        697..719
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1586 AA;  163430 MW;  15137E1F76C21618 CRC64;
     MASRPRGAPP SARPYPTQSG VAVAPRIQVL PPLPALIAWP VSLATAAGEA AGAALASAAR
     WGQHAVHEAL VGLPADIAEA AAVLVDVGKH RTRRRVWSRP GRAHIEVRGL TGHGDRHQRL
     VRGLTTVLRE TEGVRWAAVN AVLGQVVVDV EEDGVDLDQL LELVERVELE HGTSTEPFAG
     TRPYPPFESA PATLAKTSLA ADCLGLAVAA VRQVTPLPAL PPMLRVPVVV ADAQPRVRRL
     LEARLGRAHA DMLLGVSNAA VHSLTMGVAP LALDAVQRLL QLSEIRSRQA VWQLREAELV
     RTGDKLPREA PDPSARPVPL PAGPVETCGD RTSLAALLGA GGLLAWTHSP EQAAEAILAT
     VPKAAGMGRE AFASRLAGDL ARDGVVPMDG GALRLLDRIS TVLIDSAALC TARLRLLSVT
     ATGDLDEAGL WSAAQSVLTG RPLPELCGEG PWTHGRWRLE RPADAPQRRP DDPSALPLDL
     YDTDGRHQAR ILVGCELDPL ADALLGAARS GTRRLLLTEH ASAAELLPWA DHALPLGPEP
     LHEQVRRLQG EGQGVLLISA GQDHALAAAD LGVAVLPRPG AATGAVCWSA DLICGPGLAQ
     PWRILTALDE ADRVSSRSAH LSMGGSALGA LLAAAGTRRR VAGLTTSPVY GAAFLAVLGG
     MSAARRVARQ PLPPVRVRGD WHALGPLETL DTLQALHDSQ SGGQSGGEPG AQPSRRSAEQ
     PSAPRHPLYG TLQEALRTLV GLPLLGTTAL GAASLLAAVR EELRDPLTPV LALGAAASAA
     VGSSVDSALV GGVMVGNAVV SGAQRLRAER ALSGLILGER VTARRVDWAP PARTAADRTL
     LPAGLEAAPA RLATAEDLRV GDIIALRPSD VVPADARLLV SDRLELDEAV LTGESGPVAK
     DPRATPGADL AERSCMVYQG CTVLAGTGYA VVVADRAQSE AGRAADLAGR ATVPIGVEGH
     LAALTKAALP AVGVGGAVVT LLGLLRGVPV REALASGVAI AVAAVPEGLP LVATVAQSAA
     ARRLSQRGVL TRSARVLEAL GRVDVVCFDK TGTLTEGRPA VTRVTGLDHD LLLDSPAGHH
     LLRIAARACP QARPGQVLAH ATDQAVVDAA VAQCGQDQAW QPVTELPFEA SRGYAASLGI
     ESGQPCLAVK GAPETVLARC TTSLGARLGY GGDPVPLDAT GRRSAHDLVQ RLASDGLRVL
     AVAEARPAPA AAPADGEPLL VSDLTLLGFL AIADTTRPGA AETVKRLSDA GVRVAMITGD
     HPTTASAVAR ELGIPQAETV LTGSDMDTLP DGERSERIAR TTVFARVSPE HKVRIVRALQ
     QAGHVVAMTG DGVNDAAAIR LADVGIGLSA HGSTSARAAS DLVLTEPDPT RILDALLEGR
     TLWRSVRDAV AILVGGNAGE VAFTVLGTAL AGRAPLGTRQ LLLVNLLTDM LPALAVALAP
     ARRRRADEDP LADGPSPSLL GRDLARILTV RGTATTLGAA SAWQIGRVTG LSRRAGTMGL
     AALVATQLGQ TLITDWHSPL VLATSSLSAA ALIGIVETPG LSHFFGCTPL GPLAWTTVGV
     CSTTATLAAA VAPRLLSRSG PGTAPA
//
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