ID M4REB5_9BIFI Unreviewed; 864 AA.
AC M4REB5;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Copper-translocating P-type ATPase {ECO:0000313|EMBL:AGH41860.1};
GN ORFNames=D805_1593 {ECO:0000313|EMBL:AGH41860.1};
OS Bifidobacterium thermophilum RBL67.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1254439 {ECO:0000313|EMBL:AGH41860.1, ECO:0000313|Proteomes:UP000011835};
RN [1] {ECO:0000313|EMBL:AGH41860.1, ECO:0000313|Proteomes:UP000011835}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RBL67 {ECO:0000313|EMBL:AGH41860.1,
RC ECO:0000313|Proteomes:UP000011835};
RX PubMed=23640377;
RA Jans C., Lacroix C., Follador R., Stevens M.J.;
RT "Complete Genome Sequence of the Probiotic Bifidobacterium thermophilum
RT Strain RBL67.";
RL Genome Announc. 1:E00191-13(2013).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
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DR EMBL; CP004346; AGH41860.1; -; Genomic_DNA.
DR RefSeq; WP_015451110.1; NC_020546.1.
DR AlphaFoldDB; M4REB5; -.
DR KEGG; btp:D805_1593; -.
DR PATRIC; fig|1254439.12.peg.1585; -.
DR HOGENOM; CLU_001771_8_0_11; -.
DR Proteomes; UP000011835; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd02094; P-type_ATPase_Cu-like; 1.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR Gene3D; 1.10.620.20; Ribonucleotide Reductase, subunit A; 1.
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; IPR008972; Cupredoxin.
DR InterPro; IPR028096; EfeO_Cupredoxin.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR012348; RNR-like.
DR InterPro; IPR011017; TRASH_dom.
DR InterPro; IPR007029; YHS_dom.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR43520; ATP7, ISOFORM B; 1.
DR PANTHER; PTHR43520:SF8; COPPER-TRANSPORTING ATPASE 2; 1.
DR Pfam; PF13473; Cupredoxin_1; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR Pfam; PF04945; YHS; 1.
DR PRINTS; PR00943; CUATPASE.
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; SSF49503; Cupredoxins; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 180..201
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 213..235
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 247..271
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 277..295
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 445..464
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 470..492
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 689..708
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 714..733
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 820..858
FT /note="TRASH"
FT /evidence="ECO:0000259|SMART:SM00746"
FT REGION 128..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 864 AA; 91706 MW; 2A9D0DC07AB6AC49 CRC64;
MGFDLFTAVI AVVLAAILTW LTLRFFFARR EGTAAKQEQG MQSADIIVKG GYEPSLITMK
PGVPITLHFD RQETGECTSH VVFSDLGLDA MLPGNAHTDV QLPALAPGDY PFACGMNMVR
GMLRVEDDGE DHSKDHREDH ADTHRRAQPA APMPNAKDAL DNERKAADER RKEIRQLTRL
VIIGTILSLP VFIVSMLHMG GHVSMPAWLT NPWLQAVLIT PVMFYCGAPI HKVGWPALIH
RSPDMNSLVS LGSAAAYLYS LVVCVAGPAL PAGSREPYFE SVGVVITLVL VGRLLESKAR
EGTGEAVHSL IKLRPRNAQT ISSAVLDQGE RAWHDPANQS TVDIDKLKVG DLVVVKAGER
IPADGVVVAG TLDIDESMIT GESASVHSSA GGTVTGATIA LNGNAVIRVS QVGGDSVLAQ
IIAMVARAQA TKAPVQQLAD RIARVFVPAV IIIAIWTFAI WASFGPQPRL AHALVTAVSV
LIIACPCALG LATPLSVTAA TGLGATNGVL VTSAKALEQA RNIRTVVFDK TGTITRGTVD
AGADPDHPSY TSDTVKPGSQ QAIAALRKAG VRTIMLSGDK AEVAGQIAKQ VGIDTVIAQV
RPDGKAYWIE RLQAQRDADK RNDELIAMVG DGINDAPALA QADLGIAIGT GTDVAMQSAD
VTLMSGDLRG VLKLINLSNA TMRNIRENYA WAFGYNVIGI PIAAGVLYPF TGWLLSPMIA
GLAMALSSVC LVLNANRLRH AHIGDDLTAG PADADTPTAA PTIIVDEHTA LNQPSDADYH
ANTVNNTDTN SKEHTMDMSH MHHMGQMAEA TPGDGNTATD PVCGMSVAMN DEAITRTYNG
TTYYFCGEHC AANFSKAPEL FLEQ
//
