ID A0A1Q2SKI1_9GAMM Unreviewed; 838 AA.
AC A0A1Q2SKI1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Copper-translocating P-type ATPase {ECO:0000313|EMBL:BAW79646.1};
GN ORFNames=TAO_0276 {ECO:0000313|EMBL:BAW79646.1};
OS Candidatus Nitrosoglobus terrae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Candidatus Nitrosoglobus.
OX NCBI_TaxID=1630141 {ECO:0000313|EMBL:BAW79646.1, ECO:0000313|Proteomes:UP000243679};
RN [1] {ECO:0000313|EMBL:BAW79646.1, ECO:0000313|Proteomes:UP000243679}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TAO100 {ECO:0000313|EMBL:BAW79646.1,
RC ECO:0000313|Proteomes:UP000243679};
RX PubMed=28072419; DOI=10.1038/ismej.2016.191;
RA Hayatsu M., Tago K., Uchiyama I., Toyoda A., Wang Y., Shimomura Y.,
RA Okubo T., Kurisu F., Hirono Y., Nonaka K., Akiyama H., Itoh T., Takami H.;
RT "An acid-tolerant ammonia-oxidizing ?-proteobacterium from soil.";
RL ISME J. 11:1130-1141(2017).
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}.
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; AP014836; BAW79646.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q2SKI1; -.
DR KEGG; ntt:TAO_0276; -.
DR Proteomes; UP000243679; 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 GO; GO:0015662; F:P-type ion transporter activity; IEA:UniProt.
DR CDD; cd02094; P-type_ATPase_Cu-like; 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; IPR045800; HMBD.
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 PANTHER; PTHR43520; ATP7, ISOFORM B; 1.
DR PANTHER; PTHR43520:SF8; COPPER-TRANSPORTING ATPASE 2; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF19335; HMBD; 2.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00943; CUATPASE.
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:UP000243679};
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 106..127
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 180..201
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 213..235
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 287..305
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 440..462
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 468..491
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 784..803
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 809..831
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 22..49
FT /note="Heavy metal binding"
FT /evidence="ECO:0000259|Pfam:PF19335"
FT DOMAIN 60..85
FT /note="Heavy metal binding"
FT /evidence="ECO:0000259|Pfam:PF19335"
SQ SEQUENCE 838 AA; 90890 MW; 5263028B58260A39 CRC64;
MANIYGQLQA CHLGSGTANP SVYICPMHPD VQQEGSGNCP KCGMNLEQKI DTSAREKTQY
TCPMHPGVMK DKPGDCPICG MALEPRTVVT LEEEKNPELV DMLKRFWISV ALVIPLVLIA
MRDMFFWEFP ENIASPQMLN FVEFGLATPI VLWGGRPFLI RGWRSVISDE IGVLALLRRF
ISWASILFIT PLIIIFVGDV IPGSFSKHLI SNSYLVTIEL WLGSIFILWS SWPYLVHSWR
PVFNLNLNMF TLISLGVVFA YAYSIVATLF PNLFPPSFRQ ESGEVDVYFE AAGVIITLVL
LGQVLEIKAR AQTRSAIKSL LGLAPRTARR VRARGIEEDI PLHFIRPGDR LRVRPGEKIP
VDGIVIEGVS SVDESMITGE SIPVQKTVDD QVIGATINNT GGLEIKVTRV GAETVLAQIV
RMVSEAQHSR APIQRLADQV AAYLVPAVVL IAIITFIIWA MFGPEPRMVH ALINCVAVLI
IACPCALGLA TPMSIMVATG KGANAGVLFK NAEVIEVMRK IDTLVIDKTG TLTEGKPVVS
QIIVINGFNG NDILRLGGSL ELVSEHPLAA AVVSKAKEKK IKLTPVRDFQ SLTGKGVIGQ
VKGRQVAIGN EKLLEELGLS PGPLSHHAEA LRVEGQTAMF VIIDGRLAGI IGITDPIKAT
TPKAIAMLHQ EGVRIIMLTG DNQATAESVA RELGITQVEA GVLPERKVEV IKQLQKEGHL
VAMAGDGIND APALAQAQVG IAMGNGTDIA IESASITLVR GDLSGIVRAR RLSHSTMQNI
KQNLFFAFIY NLLGIPVAAG LLYPFFGILL SPMVAAAAMS FSSISIIINA LRLRLIRL
//
