ID D4BM68_BIFBR Unreviewed; 878 AA.
AC D4BM68;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=Copper-exporting ATPase {ECO:0000313|EMBL:EFE89887.1};
DE EC=3.6.3.4 {ECO:0000313|EMBL:EFE89887.1};
GN ORFNames=BIFBRE_03160 {ECO:0000313|EMBL:EFE89887.1};
OS Bifidobacterium breve DSM 20213 = JCM 1192.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=518634 {ECO:0000313|EMBL:EFE89887.1, ECO:0000313|Proteomes:UP000003191};
RN [1] {ECO:0000313|EMBL:EFE89887.1, ECO:0000313|Proteomes:UP000003191}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20213 {ECO:0000313|EMBL:EFE89887.1,
RC ECO:0000313|Proteomes:UP000003191};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
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:EFE89887.1}.
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DR EMBL; ACCG02000005; EFE89887.1; -; Genomic_DNA.
DR RefSeq; WP_003828136.1; NZ_JDUD01000002.1.
DR AlphaFoldDB; D4BM68; -.
DR STRING; 1685.RY69_1800; -.
DR KEGG; bbrd:BBBR_0226; -.
DR PATRIC; fig|518634.20.peg.240; -.
DR HOGENOM; CLU_001771_8_0_11; -.
DR Proteomes; UP000003191; Unassembled WGS sequence.
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; PR00119; CATATPASE.
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 Hydrolase {ECO:0000313|EMBL:EFE89887.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000003191};
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 173..193
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 205..228
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 240..264
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 270..288
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 436..455
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 461..483
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 687..706
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 712..731
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 834..872
FT /note="TRASH"
FT /evidence="ECO:0000259|SMART:SM00746"
FT REGION 747..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 797..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..784
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 797..815
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 878 AA; 92125 MW; 2BD0E5D5521A963D CRC64;
MEFNLFSTAA ALIAAAALTW LVLRFFFGAQ KAASGAMDVS GKRQTATITV KGGYSPAVVS
MRAGTPITLT FDRQETGECT SHVVFGDLGL DAMLPGNAVT DVELPALPAG EYPFACGMNM
VHGLLKVEGN ASAGTDKLHP LTASAEAPML DSAEAERREA AERTKEITSL TRLVAIGTVL
TLPVFIVTML HMANPMLVPH WMVNPWLQAI LITPVMFYCG HPIHAVGFPA LAHRSPDMNS
LVSLGTSAAY LYSLVTCVAP QVFPEGSREP YFESVGVVIT LVLVGRLLET KAREGTGKAV
QSLIKLRPRN AHKLNAASPE NVEWLNPANF TDMDIDTIAV GDLLVVKNGE RVPTDGIIVA
GNASIDESMI TGESKPVTKT TGAAVTGATV LLKGDLVMQA TQVGANTVLS QIAAMVARAQ
ATKAPVQQLA DRIARYFVPA VMVIAIWTFA IWIALGPAPQ LAHALITAVS VLIIACPCAL
GLATPLSVTV SLGLGATNGV LVTSAKALEQ ARRIGTVVFD KTGTITRGVV DATADWNKPS
YEQDTVKEGS PEAIAALRAR GIRTVMLSGD KAEVAGRIAR EVGIDTVICE VKPDGKAYWI
AKLQRERDEN TATSGSSRAP HDLIAMVGDG INDAPALAQA DLGIAIGTGT DVAMQSADVT
LMSGDLRGVI RTINLSNATM RNIRENLGWA FGYNIIGIPI AAGVLYPFTG WLLSPMIAGL
AMALSSVCLV LNANRLHAAN INVGAADSTA GSGSSTAGIE SAGSAESANA ANATGSTTSN
APHEPTVIID DRTTLNHTNH VSDQSNNPTN KENTMDTGMH MHHNAPAGGE TATDPVCGMT
VAVNADAITR EYEGKSYYFC GEHCATNFMK APQVFLEQ
//
