ID A0A1F4Y452_9BACT Unreviewed; 869 AA.
AC A0A1F4Y452;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Cation-transporting P-type ATPase N-terminal domain-containing protein {ECO:0000259|SMART:SM00831};
GN ORFNames=A2419_01235 {ECO:0000313|EMBL:OGC88083.1};
OS Candidatus Adlerbacteria bacterium RIFOXYC1_FULL_48_26.
OC Bacteria; Candidatus Adlerbacteria.
OX NCBI_TaxID=1797247 {ECO:0000313|EMBL:OGC88083.1, ECO:0000313|Proteomes:UP000176568};
RN [1] {ECO:0000313|EMBL:OGC88083.1, ECO:0000313|Proteomes:UP000176568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {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:OGC88083.1}.
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; MEXB01000012; OGC88083.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F4Y452; -.
DR STRING; 1797247.A2419_01235; -.
DR Proteomes; UP000176568; Unassembled WGS sequence.
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 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; 2.
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; 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 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 58..81
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 87..103
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 247..271
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 277..302
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 662..682
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 694..712
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 733..757
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 769..790
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 802..823
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 835..859
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 9..83
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 869 AA; 94073 MW; 45316E4F639B743C CRC64;
MNPDIQNRNF WHLSFEETAE VFETDIEKGL SAQEVQSRLL AFGNNTISVS KKMPGLKIFL
NQLKSPLILI LIFAGIVTLA ISHYQDAIFI FVAVVVNSAL GFYQENKAER ALSELKTYLK
QRARVIRDGK EREVGAEELV PGDIIRLAQG DRVPADARVM FANDFQVDEA VLTGESLPVS
KSTDASPESA GLSDQTSMIF AGTLVTQGIC TAIVCRTNSS TELGKVASLI AASENEKTPL
QKAIIKFSVH SSIALGALTL AVFGLGLLAG YSALDMFLTS VAIAVSAIPE GLPISMTVIL
AVGVERMAKR KGVVRKLVAA EALGSTTVIL TDKTGTLTMA KMVMSKIIPV GALDEQKLLT
RALTNANVLI ENPNDDPDSW RMNGRIMEAA LVRAAGLKGM ASAEITAKEH ILQTMPFNAV
QKFSASLVKE NGKHIVVFLG APDILAQRSS LDAKEKEAIL RHIEDLALSG ERVLGLATKE
ITDTENFSFS KDTPTHLSFN GLITFRDPIR PGIKHALSRV RGAGVKTVIL TGDHRGTAIA
VANEIGMDID DGSALDASEL STLSEEELRA RLPHLVVISR VTPFDKLRIA KLFQDMGEVV
AMTGDGVNDA PSIKQADVGI AMGSGTEVAQ SVADLVLLDD NFETIVAAIE EGRQILSNLR
KVLVYLLSNV TDGLILIGGS LLTGLPLPLN ALQILWVNFF TDSFPAVSYA FEKEPDSLSH
KPVKRGKVQL FDPVMKFLIL AIGLSTSILL FVIYYVLMQF NFDETIVRTF IFAAFGTYTL
LVALSVRSLD RSIFSYPLFS NKYLNGGILI GLVLMAAAIY VPGLQKVFDT VALPLAWVVG
VAVIGLLNVV LIEMAKGFFR YRQKMSSVR
//