ID Q73RS7_TREDE Unreviewed; 891 AA.
AC Q73RS7;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 153.
DE SubName: Full=Copper-translocating P-type ATPase {ECO:0000313|EMBL:AAS10506.1};
DE EC=3.6.3.4 {ECO:0000313|EMBL:AAS10506.1};
GN OrderedLocusNames=TDE_0008 {ECO:0000313|EMBL:AAS10506.1};
OS Treponema denticola (strain ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153
OS / KCTC 15104).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC Treponema.
OX NCBI_TaxID=243275 {ECO:0000313|EMBL:AAS10506.1, ECO:0000313|Proteomes:UP000008212};
RN [1] {ECO:0000313|EMBL:AAS10506.1, ECO:0000313|Proteomes:UP000008212}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153 / KCTC 15104
RC {ECO:0000313|Proteomes:UP000008212};
RX PubMed=15064399; DOI=10.1073/pnas.0307639101;
RA Seshadri R., Myers G.S., Tettelin H., Eisen J.A., Heidelberg J.F.,
RA Dodson R.J., Davidsen T.M., DeBoy R.T., Fouts D.E., Haft D.H., Selengut J.,
RA Ren Q., Brinkac L.M., Madupu R., Kolonay J., Durkin S.A., Daugherty S.C.,
RA Shetty J., Shvartsbeyn A., Gebregeorgis E., Geer K., Tsegaye G., Malek J.,
RA Ayodeji B., Shatsman S., McLeod M.P., Smajs D., Howell J.K., Pal S.,
RA Amin A., Vashisth P., McNeill T.Z., Xiang Q., Sodergren E., Baca E.,
RA Weinstock G.M., Norris S.J., Fraser C.M., Paulsen I.T.;
RT "Comparison of the genome of the oral pathogen Treponema denticola with
RT other spirochete genomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:5646-5651(2004).
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; AE017226; AAS10506.1; -; Genomic_DNA.
DR RefSeq; NP_970625.1; NC_002967.9.
DR RefSeq; WP_002680864.1; NC_002967.9.
DR AlphaFoldDB; Q73RS7; -.
DR STRING; 243275.TDE_0008; -.
DR PaxDb; 243275-TDE_0008; -.
DR GeneID; 2741623; -.
DR KEGG; tde:TDE_0008; -.
DR PATRIC; fig|243275.7.peg.9; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_0_3_12; -.
DR OrthoDB; 9760364at2; -.
DR Proteomes; UP000008212; 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:0005507; F:copper ion binding; IEA:InterPro.
DR CDD; cd00371; HMA; 2.
DR CDD; cd02094; P-type_ATPase_Cu-like; 1.
DR Gene3D; 3.30.70.100; -; 2.
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; IPR017969; Heavy-metal-associated_CS.
DR InterPro; IPR006122; HMA_Cu_ion-bd.
DR InterPro; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_sf.
DR InterPro; IPR027256; P-typ_ATPase_IB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01511; ATPase-IB1_Cu; 1.
DR NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR NCBIfam; TIGR00003; copper ion binding protein; 2.
DR PANTHER; PTHR43520; ATP7, ISOFORM B; 1.
DR PANTHER; PTHR43520:SF8; COPPER-TRANSPORTING ATPASE 2; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00403; HMA; 2.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00943; CUATPASE.
DR PRINTS; PR00942; CUATPASEI.
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 SUPFAM; SSF55008; HMA, heavy metal-associated domain; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 2.
DR PROSITE; PS50846; HMA_2; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362081};
KW Cell membrane {ECO:0000256|RuleBase:RU362081};
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Copper transport {ECO:0000256|ARBA:ARBA00022796};
KW Hydrolase {ECO:0000313|EMBL:AAS10506.1};
KW Ion transport {ECO:0000256|ARBA:ARBA00022796};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362081};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU362081};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW Reference proteome {ECO:0000313|Proteomes:UP000008212};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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}; Transport {ECO:0000256|ARBA:ARBA00022796}.
FT TRANSMEM 110..131
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 143..161
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 182..200
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 220..238
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 375..394
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 406..427
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 729..748
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 754..776
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 3..69
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 827..891
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 75..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 891 AA; 94685 MW; ACE6BD0430896CF1 CRC64;
MGKKIKFNIT GMTCSACSSH VQRAVEKLEG AAEVQVNLLT NSMSVNYDEA ILGTDKVIEA
VEKAGYGASL AEGLKNSSSN KNSADGKTSG SRSFQNDAAK LERDKIKKRL ILSLVFMIPL
FYVSMGHMAS LPIPHFLHGI ENALIFSFTQ FLLALPVLII NKKFFTGGFK AFLNKAPNMD
SLVAVGSGAA LIYGIFAIYK MAYGMGHGDM ETVRLFAGDL YFESAAMILT LVSLGKFLEA
NAKGKTSQAI TKLMNLRPKT ALVIRNSNEE EIPVEEIVKG DLILIKPGFS IPVDGIIVEG
NSSVDEAAIT GESLPVEKTA GDKVVSASIN LSGTFTFKAE RVGDDTTLSQ IIALVEEASA
SKAPVSKLAD KISNYFVPAV IAIAVITLFI WLIAGEGFEF ALSRAISVLV ISCPCALGLA
TPTAIMAGTG KGARLGILIR SAEALETAHK TNTVVLDKTG TITQGRPDVI DIKKTENFSE
DEVLSLAYSL EVLSEHPLAN AVIKRAKEKN LEALKIKDFK AEHGFGISGI EEASGLKIFA
GNEKLFQKNN IEISHAKAEI DALAEKGATP LLIGVSGGAG RSASETDTGA KLIGIIAVAD
KIKEGSIESI AEFKAMGIRT IMLTGDNKKT ANAIKAQTGV DDFAAELLPQ NKKNEIEKLH
QAGLKTAMIG DGINDAPALM TADVGIAIGN GTDIAIESAD IILMNDNLQT AVDSIQLSRA
VMRNIKENLF WALFYNSLCI PLAAGVFYPL FGIVLSPMIA AAAMSLSSVS VVSNALRLNY
FKPKRKCKIS RDAGPVSSSS AESESNCTVN TESCAADKNK IKEKELMNTV LKVNGMQCQH
CVSHVKEALT KISGVSAEID LGAKTATITH PESVSVADLK KAIEDAGYTV E
//
