ID A0A133XW09_9ACTN Unreviewed; 906 AA.
AC A0A133XW09;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Putative potassium/sodium efflux P-type ATPase, fungal-type {ECO:0000313|EMBL:KXB35116.1};
GN ORFNames=HMPREF3192_00481 {ECO:0000313|EMBL:KXB35116.1};
OS Atopobium deltae.
OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales; Atopobiaceae;
OC Atopobium.
OX NCBI_TaxID=1393034 {ECO:0000313|EMBL:KXB35116.1, ECO:0000313|Proteomes:UP000070675};
RN [1] {ECO:0000313|Proteomes:UP000070675}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DNF00019 {ECO:0000313|Proteomes:UP000070675};
RA Mitreva M., Pepin K.H., Mihindukulasuriya K.A., Fulton R., Fronick C.,
RA O'Laughlin M., Miner T., Herter B., Rosa B.A., Cordes M., Tomlinson C.,
RA Wollam A., Palsikar V.B., Mardis E.R., Wilson R.K.;
RL Submitted (JAN-2016) 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}.
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:KXB35116.1}.
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DR EMBL; LSCR01000006; KXB35116.1; -; Genomic_DNA.
DR RefSeq; WP_066304920.1; NZ_KQ959487.1.
DR AlphaFoldDB; A0A133XW09; -.
DR STRING; 1393034.HMPREF3192_00481; -.
DR PATRIC; fig|1393034.3.peg.461; -.
DR OrthoDB; 9814270at2; -.
DR Proteomes; UP000070675; 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; 3.
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; PR00120; HATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 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:UP000070675};
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 60..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 83..102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 269..292
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 304..332
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 694..719
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 765..786
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 844..861
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 867..893
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 2..76
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 906 AA; 97513 MW; 0B60E6B95DF6E1D5 CRC64;
MKEYLTDAQD VVDGLNSSTQ EGLTSTDAQQ RLTEHGPNKL KQAEKDPLYK RFFAQMADPM
IIMLIIAACI SAIEGLYKGS ADFADVIIIM FVVILNSVLG VVQEAKAEEA LAALQEMTAA
ASKVIRDGKQ LQVPSAELVV GDIVLLEAGD AVPADCRILE SASLKIEEAA LTGESVPVSK
FVDTLNLGQT AQAEQGQDAQ SSGAPSSDIP LGDRKNMCYM GSTVVFGRGR AVVVATGMDT
EMGKIADALT QAEDGQTPLQ RKLSELSHVL TILVVGISVA IFLTGFLKYG LAFLSNFDHV
LDTFMIAVSL AVAAIPEGLV AVVTIVLSLG VTKMSQQRAI IRKLSAVETL GSTQIICSDK
TGTLTQNKMT VVECATNDID EHVRAMALAS DAVWDDQANE AVGEPTEAAL VADAAKKGFV
TSALRTQYPR VGEAPFDSGR KMMSVVVRTQ EGFMQYTKGG PDVVLARCTK YLSADGVIDM
TDEIRATIMQ QNKELADKAL RVMASASRSW GLTQPASFAP SELEHDLTFV GLSGMIDPVR
PEVKMAVAQA KSAGIRVVMI TGDHIDTAVA IAKELDIIQD RTQAISGTQL DKLSDEELAA
HIADYGVYAR VQPEHKVRIV DAWQKQNKIV GMTGDGVNDA PSIKRADIGI GMGITGTDVT
KNVADMVLAD DNFATIIGAV EEGRRIYDNI RKCIQFLLSS NLAEVISVFV ASLVGFTILE
PTHLLWINLI TDSLPALAMA TEPAEPNIMT RRPRDAKDGI FSGGLSIDTI VQGVLIAALT
LVSYFIGHWY EFGTFDISQV LIDPTAGKDG MTMAFLTLSM VEMFHSLNMR SRRQSLFVLK
KQNIWIWAAF GMALILTFVV IETPLSAAFG FAEIDVVEYG IAMLLAALII PLVEAEKALM
RSLDKN
//
