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Database: UniProt
Entry: A0A420UU50_9ACTN
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ID   A0A420UU50_9ACTN        Unreviewed;       917 AA.
AC   A0A420UU50;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Cation-translocating P-type ATPase {ECO:0000313|EMBL:RKM90707.1};
GN   ORFNames=DC095_031830 {ECO:0000313|EMBL:RNC68536.1}, SFRA_031550
GN   {ECO:0000313|EMBL:RKM90707.1};
OS   Streptomyces xinghaiensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1038928 {ECO:0000313|EMBL:RKM90707.1, ECO:0000313|Proteomes:UP000028058};
RN   [1] {ECO:0000313|EMBL:RKM90707.1, ECO:0000313|Proteomes:UP000028058}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19609 {ECO:0000313|EMBL:RKM90707.1,
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).
RN   [2] {ECO:0000313|EMBL:RKM90707.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 19609 {ECO:0000313|EMBL:RKM90707.1};
RA   Danilenko V.N., Bekker O.B., Vatlin A.;
RT   "Genome sequencing of Streptomyces fradiae ATCC 19609.";
RL   Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:RNC68536.1, ECO:0000313|Proteomes:UP000245280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OlgR {ECO:0000313|EMBL:RNC68536.1,
RC   ECO:0000313|Proteomes:UP000245280};
RA   Danilenko V.N., Bekker O.B., Vatlin A.;
RT   "Genome sequencing of Streptomyces xinghaiensis (fradiae) OlgR.";
RL   Submitted (OCT-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}.
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:RKM90707.1}.
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DR   EMBL; JNAD02000023; RKM90707.1; -; Genomic_DNA.
DR   EMBL; QFBD02000023; RNC68536.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A420UU50; -.
DR   OrthoDB; 9814270at2; -.
DR   Proteomes; UP000028058; Unassembled WGS sequence.
DR   Proteomes; UP000245280; 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   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; 2.
DR   PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR42861:SF29; SECRETORY PATHWAY CALCIUM ATPASE, ISOFORM G; 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; 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   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
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        53..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        75..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        230..249
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        255..282
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        690..711
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        763..785
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        822..840
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        852..871
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          7..70
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          334..357
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          379..412
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          882..917
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        385..402
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   917 AA;  94905 MW;  BBA18E28608B7132 CRC64;
     MVRDEQAPVA APPAAGLSAA EAAARLERYG PNIVSTARPT PLWHRIGTQL RDPLILVLLV
     AIALTIATGD YLDTSIISFV VVVNTAVGVT QEVRAERAVM ALRELSAPGA RVVRSGEERH
     VPSSEVVPGD LVLLGEGDIV PADGELLEEA ALLVDESSLT GEAEPVGKPL PADGEQRPVV
     SAGTVVVRGR ARFVVTATGA DSATGRIAAL MTTKPGATPL QRRLAAFGRV LAAVAVALCL
     VVLVIGLLRG QDPELMAVTA ISLVVAAVPE SLPAVVTLGL ALGARRMAER NAIVRRLPAV
     ETLGSVTVIA TDKTGTLTEG RMSAQRLWTR HGTAAVSGTG YSPEGRVERE DTELRPDTAP
     DVTELLTAAV LCNDAALQAP DASDAPDGGD RRSGEARSSA RGGEADWHAL GDPTEAALLT
     AGARLGLDRE ALAREWPRTE EVPFTSDRAR MTTVHRRPGG GLRVVCKGAP EVVLVPEVLA
     DGAGTLSEAA EAAGQLAAEG YRVLAVAVAD RAEPPEDGGD WESGLNLLGL IGILDPPREA
     AAETVAACRR AGIIPVLITG DHPLTAGVVA RRLGIVEAGE EAEEVTTGDR IRDGSAGDLT
     RPRVFARTSP EQKLDIVQAW RGAGHVVAMT GDGVNDGPAL HRADIGVAMG RRGTEVARQA
     ADLVLADDDL GTVVAAVEEG RRVYANVRRF LLYGLAGGAA EILVMLFGPF LGMPLPLLPA
     QILWINLLTH GLPGVALGAE PVAPDTMRQP PRPPEESVLG AGLWPRILAM GLVIAGASLG
     VGIWAHETGR PWQTMVFLVL GATQLGVGLA SRARPGTFTN PFLLVGIAAA LALQIAGVYL
     PPLQKLLGTE ALSAGDLLIG CALSAVGYAA MRLQVRLSAR AGRSAGPEAP EASEASEAAG
     DPGTPGVPED RERAAGR
//
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