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Database: UniProt
Entry: A0A1A0U8E2_9MYCO
LinkDB: A0A1A0U8E2_9MYCO
Original site: A0A1A0U8E2_9MYCO 
ID   A0A1A0U8E2_9MYCO        Unreviewed;       850 AA.
AC   A0A1A0U8E2;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=ATPase {ECO:0000313|EMBL:OBB67276.1};
GN   ORFNames=A5758_12545 {ECO:0000313|EMBL:OBB67276.1};
OS   Mycobacterium sp. 852014-50255_SCH5639931.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1834112 {ECO:0000313|EMBL:OBB67276.1, ECO:0000313|Proteomes:UP000092113};
RN   [1] {ECO:0000313|EMBL:OBB67276.1, ECO:0000313|Proteomes:UP000092113}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=852014-50255_SCH5639931 {ECO:0000313|EMBL:OBB67276.1,
RC   ECO:0000313|Proteomes:UP000092113};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-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:OBB67276.1}.
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DR   EMBL; LZSV01000017; OBB67276.1; -; Genomic_DNA.
DR   RefSeq; WP_067739652.1; NZ_LZSV01000017.1.
DR   AlphaFoldDB; A0A1A0U8E2; -.
DR   STRING; 1834112.A5758_12545; -.
DR   OrthoDB; 9814270at2; -.
DR   Proteomes; UP000092113; 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; 2.
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; 3.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 3.
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:SF156; CALCIUM-TRANSPORTING 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; 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   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        45..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        70..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        235..256
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        262..293
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        648..669
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        675..696
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        722..746
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        752..772
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        792..812
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        824..843
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          2..66
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
SQ   SEQUENCE   850 AA;  90990 MW;  E1C65506782D07A6 CRC64;
     MAEAGRGTAL PGLTAQEAAR RLAADGTNEL AAQKRRNLLQ EAWDVIRQPM LLLLLGAGLV
     NFLLAEPLDG IMLMGFVVVV IAISIYQEHR TERALAALRD LSSPRALVVR DGMQMRIAGR
     DVVRGDVVLL AEGDRVPADA ALLDCANFSV DESALTGESV PVRKVSIEPA TVSAAMGRPG
     GDATPWVFSG TLVVKGHGIA EVKQTGAGTE LGKIGTALRT IKPERTPLQR EIDRLVGILA
     VLGVGVAVAV VIVYGLTRGN WLAGVLAGIA TAMALLPEEF PVVLTVFLAL GAWRMSRKRV
     LTRRPPVIET LGSATVLCVD KTGTLTLNRM TVRQLIVDGQ AHSLGAGPLP EGFHAIAEFA
     VLASPVDPFD PMDKAFKELG EKYLSGTEHV HAEWELVREY PLSEKLLALS HVWRSPDGGK
     FVIAAKGAPE AIADLCHFTA DEVAALTTDV ERATAGGQRV LAVACGHFDS DTALPAEQHD
     FQFEFLGLAG LHDPVRPGVA EAVAECRRAA IRTIMITGDY PGTALAIARD IGLDHAAGCI
     TGRELDTMSD DELAHRIRSV SIFARMVPEQ KLQLVRALQA NGEVVGMTGD GVNDAPALRA
     ADIGIAMGAH GTDVARESAA LVITDDDFAS IVGGVSQGRG IFDNLRKAMS YVIAVHLPIV
     GMSLVPVFVS GWPLVLLPVQ IAFLELIIDP ACSVVFESEE IDPKIMDAPP RGLNEPMFGS
     RVLTIAALQG LSVLAVTLGV YLWAVLNERP DNVIRSVTFV ALVVGNLALI LVNRSWRLPI
     WRTFRERRNR ALKWILGATA SLLIVVLTLP GPRRAFNFGP ITPWDWLIAV AAGFIGVAWF
     EIYKAVVARR
//
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