ID X0QAB4_9LACO Unreviewed; 631 AA.
AC X0QAB4;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=P-type Cu(+) transporter {ECO:0000256|ARBA:ARBA00012517};
DE EC=7.2.2.8 {ECO:0000256|ARBA:ARBA00012517};
GN ORFNames=JCM14108_428 {ECO:0000313|EMBL:GAF35535.1};
OS Lentilactobacillus farraginis DSM 18382 = JCM 14108.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lentilactobacillus.
OX NCBI_TaxID=1423743 {ECO:0000313|EMBL:GAF35535.1, ECO:0000313|Proteomes:UP000019488};
RN [1] {ECO:0000313|EMBL:GAF35535.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 14108 {ECO:0000313|EMBL:GAF35535.1};
RA Yuki M., Oshima K., Suda W., Kitahara M., Kitamura K., Iida T., Hattori M.,
RA Ohkuma M.;
RT "Draft Genome Sequences of Two Lactobacillus Strains, L. farraginis JCM
RT 14108T and L. composti JCM 14202T, Isolated from Compost of Distilled
RT Shochu Residue.";
RL Genome Announc. 2:e00257-14(2014).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAF35535.1}.
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DR EMBL; BAKI01000002; GAF35535.1; -; Genomic_DNA.
DR AlphaFoldDB; X0QAB4; -.
DR STRING; 1423743.FD41_GL000351; -.
DR eggNOG; COG2217; Bacteria.
DR Proteomes; UP000019488; Unassembled WGS sequence.
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; 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; 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; 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 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.
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 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|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 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 38..56
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 94..113
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 250..272
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 278..301
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 584..616
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
SQ SEQUENCE 631 AA; 68151 MW; FFD69CFFB72D7C07 CRC64;
MIKISNMQKF WLSLILASPM LLQMVLMPFH WIIPGYTWIA FLTTTLIMLI SAAPYWKSAW
AAFKHHNANM NTLVAVGTSV AYFYSLFAML TGRAVYFESA ALVTVFVLLG DALEERMHSS
ASNALSKLLN LQVKEADVLT NDQYSKVPLE KVQVGDIIRV RPGEKIPVDG VVTKGTTHVN
ESMVTGESLP VSKKTGDEVI GSTINMDGLL IFRATKVGKD TALAQIVELV KKAQTSHAPI
QNLTDRLSSI FVPAVLIAAI VTFVIWFVFL GAPAVQAMLF AVSVIVIACP CALGLATPTA
LMVGTARSAK LGVLIKNGQA LEEVNHVKTV VFDKTGTITA GKPVVTDVIG NQQKVLQIAA
ALEVNSEHPL ASAVMAKAKQ YQLRYSQATD FQNIEGKGVK AAVDGQNAFV GSAKLMTTYQ
MADDLKTEMT RLQNDAKTVV LVGLAGQVIG LIAIQDTPKK TAAQAISELK ARGLKTVMLT
GDNQRVAQAI GSQVGIDQVI AGVLPNEKAD HVKALQQDGQ VAFVGDGIND APALTVADVG
IAMGSGTDIA IESGEIILMQ NDLMGVVRAL EISKKTFNRI KLNLFWAFIY NLIGIPISAG
VLVGIGLQLS LSWLVWQWLS HRFRWLLRHY Y
//