ID D7CY62_TRURR Unreviewed; 661 AA.
AC D7CY62;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Heavy metal translocating P-type ATPase {ECO:0000313|EMBL:ADI14701.1};
GN OrderedLocusNames=Trad_1582 {ECO:0000313|EMBL:ADI14701.1};
OS Truepera radiovictrix (strain DSM 17093 / CIP 108686 / LMG 22925 / RQ-24).
OC Bacteria; Deinococcota; Deinococci; Trueperales; Trueperaceae; Truepera.
OX NCBI_TaxID=649638 {ECO:0000313|EMBL:ADI14701.1, ECO:0000313|Proteomes:UP000000379};
RN [1] {ECO:0000313|Proteomes:UP000000379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17093 / CIP 108686 / LMG 22925 / RQ-24
RC {ECO:0000313|Proteomes:UP000000379};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA Ovchinnikova G., Munk A.C., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA Tindall B., Pomrenke H.G., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Truepera radiovictris DSM 17093.";
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADI14701.1, ECO:0000313|Proteomes:UP000000379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17093 / CIP 108686 / LMG 22925 / RQ-24
RC {ECO:0000313|Proteomes:UP000000379};
RX PubMed=21475591; DOI=10.4056/sigs.1563919;
RA Ivanova N., Rohde C., Munk C., Nolan M., Lucas S., Del Rio T.G., Tice H.,
RA Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA Liolios K., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Brambilla E., Rohde M.,
RA Goker M., Tindall B.J., Woyke T., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.;
RT "Complete genome sequence of Truepera radiovictrix type strain (RQ-24).";
RL Stand. Genomic Sci. 4:91-99(2011).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU362081}.
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}.
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DR EMBL; CP002049; ADI14701.1; -; Genomic_DNA.
DR AlphaFoldDB; D7CY62; -.
DR STRING; 649638.Trad_1582; -.
DR KEGG; tra:Trad_1582; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_6_3_0; -.
DR Proteomes; UP000000379; 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 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; 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; 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; 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; PS01229; COF_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362081};
KW Cell membrane {ECO:0000256|RuleBase:RU362081};
KW Coiled coil {ECO:0000256|SAM:Coils};
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:UP000000379};
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 50..67
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 105..132
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 273..291
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 303..329
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 607..632
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 245..272
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 661 AA; 67232 MW; 96F368FD93C859FF CRC64;
MSGSTNRPRR PRSRHRLATC AQGDAATRES AAEQLTPATP WYRTGAGGHA LCVGVLFAMA
VALSLALPER APWAYALTTL VGAWPLARKA ASGALAGRPF GMSTLVSLAA LGALLIGEAA
EGALVVTLFL LGERLEGVAA ARARRSVSAL AALTPKTARV LEAGGVRVLS AASLRPGQRV
RVAPGERIPA DGVVLEGAST VDESPLTGES VPRSRGVGEA VFAGSVNGEG ALTVAVTRPG
DDNLLARTQR LVDEAQRRRS RSERLIDRFS RRYTPGVLAA ALLAALLPPL VAGAAWETSL
YRALALLLIG CPCALVLGVP AAMTSALAAG ARRGLLVKGG AVFEALARVR TVALDKTGTL
SQARLEVTDV VPLGRSAEAV LELAGAVEAT SAHPLAQAIT AHARAAGLSL PEVSAAQALP
GRAVAGTVGD VRVVVASPRY AALLTPLGGA VRARVAALEA AGKTVAVTLV GGEVAGLIAL
RDAVRPEARR ATEALRALGL RVVVLTGDNR RAAAALAAPL GLEVRAELLP EAKLRLVERL
GPGVMMVGDG INDAPALARA DVGVAMGGGT DVALETADAA LLRAELTGVA DLVALARRAL
RTVRANIAIA LGLKALFLAT TLLGVTGLWA AILADTGATA LVTANALRLL RPTTAPRPGG
R
//
