ID W6T596_9LACO Unreviewed; 643 AA.
AC W6T596;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=P-type Cu(+) transporter {ECO:0000256|ARBA:ARBA00012517};
DE EC=7.2.2.8 {ECO:0000256|ARBA:ARBA00012517};
GN ORFNames=LFAB_13460 {ECO:0000313|EMBL:ETY73271.1};
OS Lactiplantibacillus fabifermentans T30PCM01.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=1400520 {ECO:0000313|EMBL:ETY73271.1, ECO:0000313|Proteomes:UP000019247};
RN [1] {ECO:0000313|EMBL:ETY73271.1, ECO:0000313|Proteomes:UP000019247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T30PCM01 {ECO:0000313|EMBL:ETY73271.1,
RC ECO:0000313|Proteomes:UP000019247};
RX PubMed=24558238;
RA Treu L., Vendramin V., Bovo B., Giacomini A., Corich V., Campanaro S.;
RT "Genome Sequence of Lactobacillus fabifermentans Strain T30PCM01, Isolated
RT from Fermenting Grape Marc.";
RL Genome Announc. 2:e00060-e00014(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:ETY73271.1}.
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DR EMBL; AWWK01000066; ETY73271.1; -; Genomic_DNA.
DR RefSeq; WP_033614446.1; NZ_KK036516.1.
DR AlphaFoldDB; W6T596; -.
DR STRING; 1400520.LFAB_13460; -.
DR PATRIC; fig|1400520.3.peg.2637; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_11_2_9; -.
DR OrthoDB; 9813266at2; -.
DR Proteomes; UP000019247; 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; 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.
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 7..23
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 35..53
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 91..110
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 247..266
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 272..298
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 581..604
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 610..629
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
SQ SEQUENCE 643 AA; 68249 MW; CA0FFFA4E1ED6298 CRC64;
MSVKNRFVFS LVVSFPMLIE MLLQPFGFSL PGHEWTMFLL TTAVMIVSAG PFLRSAWAAF
RHHHANMDTL VAVGTATAYF YSIYAMLNHQ AVFYESAAFV VTFILLGQYF EDKMKHSASG
AVEKLLDLQA KDAEVMRDGQ LVKIPLTEVV VGDLIRVKPG QKIAVDGVIT EGSSTIDESM
VTGESMPVEK RAGDSVIGAT MNNTGTFMFK ANKIGNDTLL SQIVEMVKKA QTSHAPIQKT
VDKIADIFVP TVLIIAILTF FTWYVLLGAS VVNAMLFAVS VVIIACPCAL GIATPTALMV
GTGRSAKMGI LIKNGEVLEA ANTIKTVVFD KTGTITNGKP KVTDIVGDET QVLTIAAQLE
AASEHPLAAA IMDRANAAGV TPTAATNFQA IQGKGVQAQI GAQQAFIGND KLLNDYHLTS
DLTQQMTQLQ NEAKTVVLVG LSDQVIGLIA IQDAPKPTSA TAIAELKAQG LRTVMLTGDN
ELVAQAIAKQ VGIDQVIADV LPGDKADHVK QLQTEGPVAF VGDGINDAPA LTTADVGIAM
GSGTDIAIES GGIVLVKNDL RDVVRALELS RKTFNRIKLN LFWAFIYNTL GIPVAAGLFF
GIGLSLSPEL AGLGMALSSL SVVASSLLLN KSKLTTRVDA QEA
//
