ID F9VJ60_ARTSS Unreviewed; 742 AA.
AC F9VJ60;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=P-type Cu(+) transporter {ECO:0000256|ARBA:ARBA00012517};
DE EC=7.2.2.8 {ECO:0000256|ARBA:ARBA00012517};
GN OrderedLocusNames=SFBM_0241 {ECO:0000313|EMBL:BAK56020.1};
OS Arthromitus sp. (strain SFB-mouse-Japan).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Candidatus Arthromitus.
OX NCBI_TaxID=1029718 {ECO:0000313|EMBL:BAK56020.1, ECO:0000313|Proteomes:UP000001636};
RN [1] {ECO:0000313|EMBL:BAK56020.1, ECO:0000313|Proteomes:UP000001636}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SFB-mouse-Japan {ECO:0000313|Proteomes:UP000001636};
RX PubMed=21791478; DOI=10.1093/dnares/dsr022;
RA Kuwahara T., Ogura Y., Oshima K., Kurokawa K., Ooka T., Hirakawa H.,
RA Itoh T., Nakayama-Imaohji H., Ichimura M., Itoh K., Ishifune C.,
RA Maekawa Y., Yasutomo K., Hattori M., Hayashi T.;
RT "The lifestyle of the segmented filamentous bacterium: a non-culturable
RT gut-associated immunostimulating microbe inferred by whole-genome
RT sequencing.";
RL DNA Res. 18:291-303(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Cu(+)(in) + H2O = ADP + Cu(+)(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:25792, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:49552,
CC ChEBI:CHEBI:456216; EC=7.2.2.8;
CC Evidence={ECO:0000256|ARBA:ARBA00001390};
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; AP012202; BAK56020.1; -; Genomic_DNA.
DR RefSeq; WP_005807276.1; NC_015913.1.
DR AlphaFoldDB; F9VJ60; -.
DR STRING; 1029718.SFBM_0241; -.
DR KEGG; asf:SFBM_0241; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_11_2_9; -.
DR OrthoDB; 9813266at2; -.
DR Proteomes; UP000001636; 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:0006825; P:copper ion transport; IEA:UniProtKB-KW.
DR CDD; cd00371; HMA; 1.
DR CDD; cd02094; P-type_ATPase_Cu-like; 1.
DR Gene3D; 3.30.70.100; -; 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; IPR017969; Heavy-metal-associated_CS.
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 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; 1.
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 SUPFAM; SSF55008; HMA, heavy metal-associated domain; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 1.
DR PROSITE; PS50846; HMA_2; 1.
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 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 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 85..103
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 123..144
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 343..365
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 687..709
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 715..734
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 1..67
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 742 AA; 81709 MW; 1DF0FE2B2FCE8129 CRC64;
MKKVLKITGM TCAACSSSIE KSLSRKKGVN NVVVNLSTEK LTINFDEKEI NLDQIESYVI
KLGYGIDKLS EDNYYDRENE YIRNILKRFI ISLVFTIPLL YISMGHMFSY KVIDFFDHMS
NPFNFTIAQL ILVMPVMIVG FPFFKKGIKS LINLKPNMDS LITIGTFAAF LYSLYETIKV
ILGDHSRAMN LYYESSATIL TLITLGKYLE GVTKGKTSKA IKKLMGLSPR TALIEKDGDE
VEVSIDEVKV SDIVIVKSGD KFPVDGEIIY GSCLVDESML TGESVPVYKK VSDDVIGASI
NKNGFVKYRV TKVGDNTMLS QIIKLVEEAQ NSKPKISKLA DTVSYYFVPT IIAIALLSFI
FWLIYERNFG FAFSIFVSVL VIACPCALGL ATPTSIMVST GIGAENGILI KSGKALEDAH
KINVVVLDKT GTITEGKPKV TDLIIDKDVF KDNEEMIKYV TSIEKGSEHP LGEAILEYGK
EKNIDTLDVD NFKIIEGMGV YGEVDGRKIF IGNKKLLDVN HISIDKFKDV SDDLSMHGKT
TMFVVIDEVL GGIFSVADTV KKSSKDAISK LKSMGIKVIM LTGDNFKTSF AIGNQVGIDE
VISEVLPKDK SSEVQKLRDK GYKVCMVGDG INDAPALMNS NVGISIGSGT DIAIESSSVI
LMKSDLMDIP KFLKLSKSTI GNIKQNLFWA FLYNVIGVPV AMGVFYLFGG ILLNPMISAI
AMSFSSVSVV INALRLKFIK LI
//
