ID V2RIK9_9BACT Unreviewed; 808 AA.
AC V2RIK9;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Copper-exporting P-type ATPase {ECO:0000313|EMBL:USF23225.1};
DE SubName: Full=Copper-translocating P-type ATPase {ECO:0000313|EMBL:ESJ97543.1};
GN Name=copA_1 {ECO:0000313|EMBL:USF23225.1};
GN ORFNames=N508_000281 {ECO:0000313|EMBL:USF23225.1}, N508_01466
GN {ECO:0000313|EMBL:ESJ97543.1};
OS Mucispirillum schaedleri ASF457.
OC Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC Mucispirillaceae; Mucispirillum.
OX NCBI_TaxID=1379858 {ECO:0000313|EMBL:ESJ97543.1};
RN [1] {ECO:0000313|EMBL:ESJ97543.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ASF457 {ECO:0000313|EMBL:ESJ97543.1};
RX PubMed=24723722;
RA Wannemuehler M.J., Overstreet A.M., Ward D.V., Phillips G.J.;
RT "Draft genome sequences of the altered schaedler flora, a defined bacterial
RT community from gnotobiotic mice.";
RL Genome Announc. 2:e00287-e00214(2014).
RN [2] {ECO:0000313|EMBL:USF23225.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ASF457 {ECO:0000313|EMBL:USF23225.1};
RA Proctor A.L., Phillips G.J., Wannemuehler M.J.;
RL Submitted (MAY-2022) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:USF23225.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ASF457 {ECO:0000313|EMBL:USF23225.1};
RA Proctor A., Parvinroo S., Richie T., Jia X., Lee S.T.M., Karp P.D.,
RA Paley S., Kostic A.D., Pierre J.F., Wannemuehler M.J., Phillips G.J.;
RT "Resources to Facilitate Use of the Altered Schaedler Flora (ASF) Mouse
RT Model to Study Microbiome Function.";
RL Submitted (JUN-2022) to the EMBL/GenBank/DDBJ databases.
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; AYGZ01000018; ESJ97543.1; -; Genomic_DNA.
DR EMBL; CP097562; USF23225.1; -; Genomic_DNA.
DR RefSeq; WP_023276293.1; NZ_FTRD01000001.1.
DR AlphaFoldDB; V2RIK9; -.
DR STRING; 1379858.N508_01466; -.
DR GeneID; 78587022; -.
DR PATRIC; fig|1379858.3.peg.1468; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_0_3_0; -.
DR OrthoDB; 9814270at2; -.
DR Proteomes; UP000017429; 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; 3.30.70.100; -; 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; IPR021993; ATPase-cat-bd.
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; 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 InterPro; IPR011017; TRASH_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:SF5; CATION-TRANSPORTING P-TYPE ATPASE-RELATED; 1.
DR Pfam; PF12156; ATPase-cat_bd; 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; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00746; TRASH; 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; PS01229; COF_2; 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 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:UP000017429};
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 173..192
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 212..230
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 242..264
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 270..287
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 430..448
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 460..481
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 764..783
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 91..157
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 808 AA; 89074 MW; 6563F3E88D1D13CD CRC64;
MALKDTEQEN KYICGHCSSE VNPKTGIYEK ENDKYFCCEG CRSVYHLIND EGFASFYTKR
TDWDDAAPAE QVEADEEYFE TSLEVLKNGD YSLSIVITGI RCAACIWLIE SLALKDERIK
SFRINYANHK AKIVFNPNDI SVKEVLQKIT RLGYCPLPST NIETIHDKER KDYFYRFGVA
AFFTMQVMMY SIANYTGYFK GMDDSLYFLF KLLSWVLATP VLIYSAYPFF QKSFAALKHF
HFTMDTLVAI GAGTSYLYSV AAIFLGYETY FDTSVMIITL ILLGRFIEAG AKQKGGNAVA
KLLSLKPKNV RKIICEQNGE KTYITIPIDQ LLKGDLFEIS TGSNVAADGK IIEGICEIDE
SMLTGEPMPV NKKEGCQVYA GTKLINGTCI VMAENIGIDS FLSKIAASVD DAQSSKAPIQ
DVADNFISKF VPFVLIIAFL SFIYWYFLAS VGAELSIMRA VSVLVIACPC AMGLATPLAV
ISATNKLSET GVIFKNGEAI ERYAYVNDFY FDKTGTITTG NMSVTDCKLS FSCSSVLNLI
TSAAFYSKHP ASKAIAAANE SLYECEKFEE TAGKGIIAEI KNTNIIIGSQ KFLQENSVKF
TAEYEKYIEK AIEKGWTIVC AAVNHILVGV FSISDIIREE AALTISLLQK EGNNISIITG
DSQKAANIIL GNSGINANIF ANVSPFDKGS ILQNAKDTKK TVMIGDGIND AIALTAASVG
ISMRNSTDIS IESASAVLLR NDLSIIEKSH KICRKTLRII KENLFWAFSY NFIAIPLACT
GLIHPVMSAA FMSFSSLFVV ANSVRIKK
//
