UniProt: A1A2Z9

Database: UniProt
Entry: A1A2Z9_BIFAA

LinkDB:  A1A2Z9_BIFAA 
Original site:  A1A2Z9_BIFAA

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Ontology (6)   
   GO (6)   
Gene (1)   
   KEGG GENES (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (21)   
   InterPro (15)   
   Pfam (4)   
   PROSITE (1)   
   SMART (1)   
All databases (29)   

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ID   A1A2Z9_BIFAA            Unreviewed;      1000 AA.
AC   A1A2Z9;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 117.
DE   SubName: Full=ActP copper transport ATPase {ECO:0000313|EMBL:BAF40082.1};
GN   Name=actP {ECO:0000313|EMBL:BAF40082.1};
GN   OrderedLocusNames=BAD_1301 {ECO:0000313|EMBL:BAF40082.1};
OS   Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 /
OS   E194a).
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=367928 {ECO:0000313|EMBL:BAF40082.1, ECO:0000313|Proteomes:UP000008702};
RN   [1] {ECO:0000313|EMBL:BAF40082.1, ECO:0000313|Proteomes:UP000008702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15703 / DSM 20083 / NCTC 11814 / E194a
RC   {ECO:0000313|Proteomes:UP000008702};
RA   Suzuki T., Tsuda Y., Kanou N., Inoue T., Kumazaki K., Nagano S., Hirai S.,
RA   Tanaka K., Watanabe K.;
RT   "Bifidobacterium adolescentis complete genome sequence.";
RL   Submitted (DEC-2006) 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   -!- 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}.
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DR   EMBL; AP009256; BAF40082.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1A2Z9; -.
DR   PaxDb; 1680-BADO_1424; -.
DR   KEGG; bad:BAD_1301; -.
DR   HOGENOM; CLU_001771_11_1_11; -.
DR   Proteomes; UP000008702; Chromosome.
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:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd02094; P-type_ATPase_Cu-like; 1.
DR   Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 2.
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; 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; IPR008972; Cupredoxin.
DR   InterPro; IPR028096; EfeO_Cupredoxin.
DR   InterPro; IPR009078; Ferritin-like_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   InterPro; IPR012348; RNR-like.
DR   InterPro; IPR011017; TRASH_dom.
DR   InterPro; IPR007029; YHS_dom.
DR   NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
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   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
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; SSF47240; Ferritin-like; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU362081};
KW   Cell membrane {ECO:0000256|RuleBase:RU362081};
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   Reference proteome {ECO:0000313|Proteomes:UP000008702};
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}.
FT   TRANSMEM        20..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        207..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        235..257
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        269..288
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        300..317
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        451..473
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        479..506
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        825..844
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          957..995
FT                   /note="TRASH"
FT                   /evidence="ECO:0000259|SMART:SM00746"
FT   REGION          157..199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1000 AA;  104492 MW;  42DA996544405DD6 CRC64;
     MVFAEIESQL RTEGGWNMHI AIALIMALLV TAGVLWFFFA PRKAYRAPLR DGVQEAVVEV
     KGGYNPAVIE AEAGMPLRLI FDRKEDGECS SHVVFSDFGV DLALPAFRTT TLTLHPDEPG
     EYPFACGMNM LHGMLRVLPG RHAGAGADAT AGIATTAANT SMPDSGNSDM HSTTGGGHTS
     DSDETDAQTA QKNAQTPDSG ETDIRALVAR LVVAAVCTIP VFGSTMLMLY PMPNWLQFLL
     MLPIVGYAAL PIFRSGFAAI AHRSPEMNAL VSLGALAAFA YSCVVTFAPN VLPENAREPY
     FEAVGVVVTL MLVGQLLEAR ARKGTGEAMR ALAGLQPKTA RVVRDGKETS IAIDDVRVGD
     VIAIRPGEQL PVDGIVISGT STVGESMITG EAMPVAKTEG SEVTGATING GGSLRYRATK
     VGKDTVLAQI IDMVTAAQSS KAPVQRLADR ISGVFVPAVV LVAVWSCALW FAFGPEPRVT
     HALVAAVSVL LIACPCALGL ATPLSVTVST GRAARMGVLV RSAEALETCG KVNAVVLDKT
     GTITAGKPTL TDVLPFGKWR RQADDFLTIV AAAERDSEHP LAVAIVATAA EHVDAADAAQ
     TTDFQAIAGR GVTARVTFRG LPHTVAVGNT DLIDDLDVDM PDVTSDTSEI ASETIHDTNL
     DAIIADMELL SQQGKTPILA AIDGHLAGIV AVADVPKADS RQAIELLRKR GVEAVMLTGD
     NPTTARAIAS QVGIDERHVI AGVRPERKAD EIAKLQSQGY TVAMVGDGIN DAPALARANV
     GFAIGTGTDV AVQSADVTLM GGSLMGLVHA LDLTHAAMRN IAQNLGFALG YNSIGIAIAA
     GVLYPFTGTL LNPMIAGAAM AFSSLCVVTN ASRLRLFDPD AEAAKNKTYR VRKPDPSKNN
     GNQHSRKGTI MGLFSDHKAK KEAENMGTMG AGHCCGGHDG HGMASNMGDS AANVAKDPVC
     GMSVDPATAA ATREYGGVTY YFCNPGCADK FAQNPAAYLG
//

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