ID Q1AV18_RUBXD Unreviewed; 639 AA.
AC Q1AV18;
DT 11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 115.
DE SubName: Full=Heavy metal translocating P-type ATPase {ECO:0000313|EMBL:ABG04760.1};
GN OrderedLocusNames=Rxyl_1801 {ECO:0000313|EMBL:ABG04760.1};
OS Rubrobacter xylanophilus (strain DSM 9941 / NBRC 16129 / PRD-1).
OC Bacteria; Actinomycetota; Rubrobacteria; Rubrobacterales; Rubrobacteraceae;
OC Rubrobacter.
OX NCBI_TaxID=266117 {ECO:0000313|EMBL:ABG04760.1, ECO:0000313|Proteomes:UP000006637};
RN [1] {ECO:0000313|EMBL:ABG04760.1, ECO:0000313|Proteomes:UP000006637}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9941 / NBRC 16129 / PRD-1
RC {ECO:0000313|Proteomes:UP000006637};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., da Costa M.S.,
RA Rainey F.A., Empadinhas N., Jolivet E., Battista J.R., Richardson P.;
RT "Complete sequence of Rubrobacter xylanophilus DSM 9941.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
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; CP000386; ABG04760.1; -; Genomic_DNA.
DR RefSeq; WP_011564776.1; NC_008148.1.
DR AlphaFoldDB; Q1AV18; -.
DR STRING; 266117.Rxyl_1801; -.
DR KEGG; rxy:Rxyl_1801; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_6_4_11; -.
DR OrthoDB; 7059309at2; -.
DR PhylomeDB; Q1AV18; -.
DR Proteomes; UP000006637; Chromosome.
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; TIGR01525; ATPase-IB_hvy; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
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; SFLDS00003; Haloacid_Dehalogenase; 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:UP000006637};
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 92..110
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 239..257
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 263..289
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 594..613
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 619..637
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
SQ SEQUENCE 639 AA; 65885 MW; C75080C9F140078F CRC64;
MRHLKRLWRD PARRRLALTV SSGALIGASL MAGHGPGPES AAYPLMVAAA LVAGSDIASR
AWSSLRARHV GIELLVTIAA GGALVIGEAW EAAAVTFLFL LGATLEAHTM ERTRRTLRGL
LELAPESAVV LRGGRQVEVP PQSVARGEVV IVRPGATIPV DGVVVGGRAS VDEHAVTGES
LAVEKGAGAP VYAGAIVQDG LLRVRAEGVG AETTLARIIR RVEEAQEERV PVQRFIDRFA
RWYTPAIIGL SAAAGTLTGD VRLALTLLVI GCPGALVIAA PVAVVAGIGR AAQRGILIKG
GAHLERAGEI TALALDKTGT LTEGRPRLTE VVALSPAPAL AGGGALTGAD GSPWDAARQE
VLRWAAAAES GSEHPLARPI VEAAGELGPV PQAEGARISA GRGITATYGD HIIAVGTPGL
MEELGIEVSD EARAVLERLR RGGRTAVLVA LDGLILGVLG IADTLRAGAR EAVEGLRRAG
VRRIEMLTGD NLQTARAIAG AAGVDAVHAE LLPDEKLERI RELQRERHVV AMVGDGINDA
PALAAADVGI AMGAAGTDVA IETAPVALMG DDLGRLPEAV RLSRATLRVI RQNLAVALLT
VTGLLLGVLA GHVDMAGGML VHQLSVLLVV LNGVRLLRA
//
