ID F5VDN2_9LACO Unreviewed; 636 AA.
AC F5VDN2;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=P-type Cu(+) transporter {ECO:0000256|ARBA:ARBA00012517};
DE EC=7.2.2.8 {ECO:0000256|ARBA:ARBA00012517};
GN ORFNames=NIAS840_00668 {ECO:0000313|EMBL:EGL98950.1};
OS Ligilactobacillus salivarius NIAS840.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Ligilactobacillus.
OX NCBI_TaxID=1029822 {ECO:0000313|EMBL:EGL98950.1, ECO:0000313|Proteomes:UP000006227};
RN [1] {ECO:0000313|EMBL:EGL98950.1, ECO:0000313|Proteomes:UP000006227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIAS840 {ECO:0000313|EMBL:EGL98950.1,
RC ECO:0000313|Proteomes:UP000006227};
RX PubMed=21914873; DOI=10.1128/JB.05688-11;
RA Ham J.S., Kim H.W., Seol K.H., Jang A., Jeong S.G., Oh M.H., Kim D.H.,
RA Kang D.K., Kim G.B., Cha C.J.;
RT "Genome Sequence of Lactobacillus salivarius NIAS840, Isolated from Chicken
RT Intestine.";
RL J. Bacteriol. 193:5551-5552(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}.
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:EGL98950.1}.
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DR EMBL; AFMN01000001; EGL98950.1; -; Genomic_DNA.
DR RefSeq; WP_003705598.1; NZ_AFMN01000001.1.
DR AlphaFoldDB; F5VDN2; -.
DR PATRIC; fig|1029822.3.peg.667; -.
DR Proteomes; UP000006227; 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 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..87
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 93..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 582..605
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 611..630
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
SQ SEQUENCE 636 AA; 68716 MW; 1F3B5B7A9201701D CRC64;
MTIRARFWIS LIFSLPMFFE MILKPFGWML PGHTYTMFVL TTIVMAISAR PFLHSAWAAF
KNHHANMDTL VAIGTATAYV YSIYAMFTGQ DVFFESAAFV ITFILLGQVF EEKMRNNANS
SVEKLLNLQV KEAEVIVDGK SQMVPLDDIK VGDVIRVKPG QKIAVDGEII EGSSTVDESM
ITGESMPVTK KVGDKVIGST LNNTGTFLFK ADKVGKDTML AQIVEMVKKA QNSHAPIQKT
ADKIANIFVP VVLIIAILTY LVWYVFLGNS NVTSLLFAVS VVIIACPCAL GIATPTALMV
GTGRSAKMGI LIKDGEVLEA TDKIDTVVFD KTGTITEGKP KVTDIIGNKD EILQIAASLE
KNSEHPLATA IMDKAVEQQI KLFEVNNFTA VEGKGITGII DEQRVVVGNT KLIEDWNISQ
ELQAQMKNLQ SDAKTVVVVG KNDEVIGLIA IQDIPKATSA KAISDLKKRG LKTVMLTGDN
QQVAEVIANE VGIDEVIADV LPQDKAHHIE MLQDQGRNVA FVGDGINDAP ALTTANVGIT
MGAGTDIAIE SGGIVLVKND LEDVVKALMM SEKTFNRIKL NLFWAFIYNG LGIPVAAGIF
SGIGLTLSPE LAGLAMAFSS ISVMISSLML NRVKIA
//