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Database: UniProt
Entry: A0A3R7ETX8_9ACTN
LinkDB: A0A3R7ETX8_9ACTN
Original site: A0A3R7ETX8_9ACTN 
ID   A0A3R7ETX8_9ACTN        Unreviewed;       905 AA.
AC   A0A3R7ETX8;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   28-JAN-2026, entry version 24.
DE   SubName: Full=Cation-transporting P-type ATPase {ECO:0000313|EMBL:RKM96153.1};
GN   ORFNames=SFRA_013955 {ECO:0000313|EMBL:RKM96153.1};
OS   Streptomyces xinghaiensis.
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1038928 {ECO:0000313|EMBL:RKM96153.1, ECO:0000313|Proteomes:UP000028058};
RN   [1] {ECO:0000313|EMBL:RKM96153.1, ECO:0000313|Proteomes:UP000028058}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19609 {ECO:0000313|EMBL:RKM96153.1,
RC   ECO:0000313|Proteomes:UP000028058};
RX   PubMed=25477406;
RA   Bekker O.B., Klimina K.M., Vatlin A.A., Zakharevich N.V., Kasianov A.S.,
RA   Danilenko V.N.;
RT   "Draft Genome Sequence of Streptomyces fradiae ATCC 19609, a Strain Highly
RT   Sensitive to Antibiotics.";
RL   Genome Announc. 2:0-0(2014).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + phosphate + H(+); 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:ARBA00049360};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IIA subfamily. {ECO:0000256|ARBA:ARBA00005675}.
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:RKM96153.1}.
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DR   EMBL; JNAD02000005; RKM96153.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3R7ETX8; -.
DR   Proteomes; UP000028058; Unassembled WGS sequence.
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   CDD; cd02080; P-type_ATPase_cation; 1.
DR   FunFam; 3.40.50.1000:FF:000028; Calcium-transporting P-type ATPase, putative; 1.
DR   FunFam; 2.70.150.10:FF:000160; Sarcoplasmic/endoplasmic reticulum calcium ATPase 1; 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; IPR059000; ATPase_P-type_domA.
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; 3.
DR   PANTHER; PTHR42861; 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   Pfam; PF08282; Hydrolase_3; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00120; HATPASE.
DR   SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028058};
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        246..264
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        276..301
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        704..729
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        735..753
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        773..795
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        807..826
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        838..860
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        880..896
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          5..79
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
SQ   SEQUENCE   905 AA;  95049 MW;  83B88F84185C9163 CRC64;
     MPTEAHHGLA AHEVVMLLET DPHRGLDEGE VARRQERYGP NVLPAATGGG LLLRVLRQFH
     HPLIYVLLAA GTITALLHEY TDSAVIFGVV VVNAVVGFVQ ESKAEAALDA LRSMVRTRAR
     VVRGGRERMV PSQELVPGDL VLVEAGDKVP ADVRLIRPVS LRVDESALTG ESVPVAKDET
     VLPATAAVAD RHNMLYSGTL VTAGSGTGVT VATGAETELG AIHRLVGSAE TLVTPLTAKL
     NQFSKVLTVA ILALAALTFG IGLARGQDGA ETFTAAVALA VGAIPEGLPA AVTITLAIGV
     ARMARRKAVV RQLPAVETLG STTVIGSDKT GTLTENQMTV RAVWTPDGAE YEVTGSGYAP
     QGEIVHGTDG TVAVPRPRSA LWWTLLAGAA CNDAALTHEE GRWGLVGDPT EGALLVAAAK
     GGLDPAALPG EYARAGTLPF SSERQFMATL HRDPGSGGGT GHVVLVKGAV ERVLPLCGGW
     LAGDGTVREL DADAVLRAAE DLASRGLRVL ATAVRTDSDP RVFDEDVLDG TLTLTGLQAM
     LDPPRPAAAS AVRACHTAGI TVKMITGDHA ATAGAIAERL QLFGDVGGSR GDAGVLTGAD
     LDALPAEEYP EAVDRARVFA RVSPEQKLRL VEALQSRGHV VAMTGDGVND APALRQANIG
     IAMGRGGTEV AKEAADMVLT DDDFATIEAA VEEGRGVFDN LTKFIVWTLP TNMGEGLVIL
     AAILFGSALP ILPTQILWIN MTTAVALGLM LAFEPKEAGI MSRAPRDPDR PLLTGALAFR
     VVLVSTLLVA GSWWLFSWER AEGAGLAEAR TAALNLFVVV ELFYLFSCRS LTRSMWHVGL
     FSNKWIIGGV TVQALGQLAI TYLPAMNTLF ETTPINGETW LRILGIAALA SLVVAVDKRL
     RRQWV
//
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