ID A0A255EM01_9ACTN Unreviewed; 1029 AA.
AC A0A255EM01;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Copper-translocating P-type ATPase {ECO:0000313|EMBL:OYN92567.1};
GN ORFNames=CGZ91_03565 {ECO:0000313|EMBL:OYN92567.1};
OS Parenemella sanctibonifatiensis.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Parenemella.
OX NCBI_TaxID=2016505 {ECO:0000313|EMBL:OYN92567.1, ECO:0000313|Proteomes:UP000216300};
RN [1] {ECO:0000313|EMBL:OYN92567.1, ECO:0000313|Proteomes:UP000216300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NML 150081 {ECO:0000313|EMBL:OYN92567.1,
RC ECO:0000313|Proteomes:UP000216300};
RA Bernier A.-M., Bernard K., Domingo M.-C.;
RT "Draft whole genome sequences of clinical Proprionibacteriaceae strains.";
RL Submitted (JUL-2017) 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}.
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:OYN92567.1}.
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DR EMBL; NMVJ01000001; OYN92567.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A255EM01; -.
DR OrthoDB; 7059309at2; -.
DR Proteomes; UP000216300; 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: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; 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; 2.
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; 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; PF13473; Cupredoxin_1; 2.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR Pfam; PF04945; YHS; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00120; HATPASE.
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; 2.
DR SUPFAM; SSF47240; Ferritin-like; 1.
DR SUPFAM; SSF56784; HAD-like; 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:UP000216300};
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 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 361..384
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 390..408
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 545..564
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 570..593
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 884..903
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 909..930
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 982..1020
FT /note="TRASH"
FT /evidence="ECO:0000259|SMART:SM00746"
FT REGION 248..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 952..978
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 956..970
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1029 AA; 108129 MW; DF80C0E4898CC3A8 CRC64;
MNLNDWLVVG VALAVTVLLG WYFFGPKKSR RAEVADGVQE VTVTVKGGYS PDLIEVQPGV
PVRLVFDRQE SGECSSRVVF PDFKINQTLP ANAQTAVQFL PEVPGEYTFA CGMNMLHGRV
RVVDRPGPTT MIPTETAVAV TDQPRPVTDV PTEPAPGVRV DDGVQVAQVT IRGGYHPDTV
RLAPGMPTRL ELTRQEQAAC SERFVVPALG VDVEVPAFAT TTVELPALPE GRHEVTCGMD
MLHGAIDVGN HDDRDHGDAR HSGTGDRATR TSPGEDAEAR ERAAEIRDLR LRVIVGTVLT
LPVLLAVMVH EFFAATWVPE ALLNSWVQLA LITPVFVYTG WPIHKTGWLA LSHRTADMNS
LITLGTIAAY GYSLVVTFAP GAVPIEAREV YYEAVGVILT LILLGRWLET KAKAGTGEAI
RALIGLQPRT ARVVRRGEEF EIGLEDVLVG DVVVVRPGEK LPVDGEVAEG SSAVDESMVT
GEPIPVTKTV GDTVIGATIN QTGAFRYTAT KVGADTMLAQ IIRLVQEAQG SKAPIQRLVD
KVSSYFVPAV IGIAIWTFVV WALVGPAPAL VFALVAAVSV LIIACPCALG LATPLSITVG
TGKGATHGVL IRSAEALETA HKLDTVVLDK TGTITQGAPA LTDVLPAEGF TETELLILVA
AVERSSEHPL AAAIVAGATG RSLDLPAATA FDSVTGQGVR ALVEGREVAV GNRRLLEGAG
VRVEAAAADR LAADGKTPMF AAIDGRFAGV IGVADTVKDG SAAAVAALQA RGIDVVMMTG
DNRATAAAIA RQVGISRVVA EVMPEHKAAE VQRLQAEGRV VGMVGDGIND APALAQADVG
SAIGTGTDVA IESSDITLIS GSLSGLVTAV DLSRATMRNI RQNLVFAFIY NGLGIPIAAG
VLYPALGWML SPMIAAAAMA LSSLSVVTNA NRLRAFTPRP IPEVTQVPAT DPVVEVGHGP
DEENTPEEKE NNMSQKPTTV TDPVCGMNVE PSAAASSLDH EGQTYYFCSN HCAESFRADP
AKYTGAGTP
//
