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Database: UniProt
Entry: A0A061LXK2_9MICO
LinkDB: A0A061LXK2_9MICO
Original site: A0A061LXK2_9MICO 
ID   A0A061LXK2_9MICO        Unreviewed;       635 AA.
AC   A0A061LXK2;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=ATPase P {ECO:0000313|EMBL:EYT56756.1};
GN   ORFNames=H490_0100295 {ECO:0000313|EMBL:EYT56756.1};
OS   Leucobacter sp. UCD-THU.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Leucobacter.
OX   NCBI_TaxID=1292023 {ECO:0000313|EMBL:EYT56756.1, ECO:0000313|Proteomes:UP000026917};
RN   [1] {ECO:0000313|EMBL:EYT56756.1, ECO:0000313|Proteomes:UP000026917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCD-THU {ECO:0000313|EMBL:EYT56756.1,
RC   ECO:0000313|Proteomes:UP000026917};
RX   PubMed=23792744; DOI=10.1128/genomeA.00325-13;
RA   Holland-Moritz H.E., Bevans D.R., Lang J.M., Darling A.E., Eisen J.A.,
RA   Coil D.A.;
RT   "Draft Genome Sequence of Leucobacter sp. Strain UCD-THU (Phylum
RT   Actinobacteria).";
RL   Genome Announc. 1:S69-S82(2013).
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 IB subfamily. {ECO:0000256|ARBA:ARBA00006024,
CC       ECO:0000256|RuleBase:RU362081}.
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:EYT56756.1}.
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DR   EMBL; APJM01000002; EYT56756.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A061LXK2; -.
DR   STRING; 1292023.H490_0100295; -.
DR   HOGENOM; CLU_001771_6_3_11; -.
DR   Proteomes; UP000026917; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd02079; P-type_ATPase_HM; 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; 3.40.50.1000; HAD superfamily/HAD-like; 1.
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; IPR027256; P-typ_ATPase_IB.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01512; ATPase-IB2_Cd; 1.
DR   NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 1.
DR   PANTHER; PTHR48085; CADMIUM/ZINC-TRANSPORTING ATPASE HMA2-RELATED; 1.
DR   PANTHER; PTHR48085:SF5; CADMIUM_ZINC-TRANSPORTING ATPASE HMA2; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 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   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU362081};
KW   Cell membrane {ECO:0000256|RuleBase:RU362081};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362081};
KW   Metal-binding {ECO:0000256|RuleBase:RU362081};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026917};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU362081};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU362081}.
FT   TRANSMEM        29..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        54..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        86..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        254..273
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        279..309
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        583..610
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   635 AA;  65383 MW;  B0AAC532134BAEC6 CRC64;
     MSAVTGSQVD EVESDDDDHD GPWWKDREIL LPVFSGVAFL TGLIFEWSGL EIPALVLFWA
     GLLAGASTFT PGAIRKLFKG KLGIGLLMTI SAIGAVILGY VEEAAALAFL YSIAEALEDK
     AMDRARGGLR ALLKLVPETA TVLQGGVFVQ VQAKELTVGQ VMVVRPGERI ATDGIVRAGR
     SSLDTSAITG ESIPVEVEPG DAVSAGAINS AGALEVETTA AGTDNSLTTI VELVEQAQTE
     KGERARLADR IARPLVPGVL ILAALVAIIG SLLGDPEVWI TRALVVLVAA SPCALAISVP
     LTVVAAIGAA SKFGVIIKSG AVFERFGTVR HVAVDKTGTL TRNEPAVTAV LTADGVTETQ
     ALAWAAALEQ HSTHPLAAAI TAAAPGVSAA ADVTEQAGHG IEGSVDGVTI TVGSPRWLDV
     GELGDRVALL EGQGMTVVIV HRGGVPVAAI GVRDELRPEV PEVVRTLTDQ GIGVTMLTGD
     NARTARALAA QAGIGDVRAE LRPEDKAAAI GELSKAESVA MIGDGINDAP ALASADIGIA
     MGATGSDAAI ESADVAFTGH DLRLIPRAFD HARRGRRIIN QNIILSLLII TALLPLALFG
     VLGLAAVVLV HEVAEVVVIL NGLRAARTRT PQLAS
//
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