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Database: UniProt
Entry: S3Y0J5_9MICO
LinkDB: S3Y0J5_9MICO
Original site: S3Y0J5_9MICO 
ID   S3Y0J5_9MICO            Unreviewed;       777 AA.
AC   S3Y0J5;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   SubName: Full=Heavy metal translocating P-type ATPase {ECO:0000313|EMBL:EPH15267.1};
GN   ORFNames=HMPREF1484_00898 {ECO:0000313|EMBL:EPH15267.1};
OS   Dermabacter sp. HFH0086.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC   Dermabacter.
OX   NCBI_TaxID=1203568 {ECO:0000313|EMBL:EPH15267.1, ECO:0000313|Proteomes:UP000014577};
RN   [1] {ECO:0000313|EMBL:EPH15267.1, ECO:0000313|Proteomes:UP000014577}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HFH0086 {ECO:0000313|EMBL:EPH15267.1,
RC   ECO:0000313|Proteomes:UP000014577};
RG   The Broad Institute Genomics Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Schmidt T.M., Dai D., Dover J.,
RA   Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Dermabacter sp. HFH0086.";
RL   Submitted (MAY-2013) 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:EPH15267.1}.
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DR   EMBL; ATFO01000007; EPH15267.1; -; Genomic_DNA.
DR   RefSeq; WP_016663814.1; NZ_KE340308.1.
DR   AlphaFoldDB; S3Y0J5; -.
DR   STRING; 1203568.HMPREF1484_00898; -.
DR   PATRIC; fig|1203568.3.peg.873; -.
DR   eggNOG; COG2217; Bacteria.
DR   HOGENOM; CLU_001771_0_3_11; -.
DR   Proteomes; UP000014577; 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   CDD; cd00371; HMA; 1.
DR   CDD; cd02094; P-type_ATPase_Cu-like; 1.
DR   Gene3D; 3.30.70.100; -; 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; IPR017969; Heavy-metal-associated_CS.
DR   InterPro; IPR006121; HMA_dom.
DR   InterPro; IPR036163; HMA_dom_sf.
DR   InterPro; IPR027256; P-typ_ATPase_IB.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_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; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00403; HMA; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00120; HATPASE.
DR   SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 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   SUPFAM; SSF55008; HMA, heavy metal-associated domain; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
DR   PROSITE; PS01047; HMA_1; 1.
DR   PROSITE; PS50846; HMA_2; 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|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU362081};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014577};
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        106..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        133..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        170..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        216..234
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        373..395
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        401..422
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        727..747
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        753..771
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          11..76
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   777 AA;  80522 MW;  001BC161D89A83EE CRC64;
     MSSTETHTAP RTVTLDVTGM TCASCVARVE KKLRRVGDVD AVVNLALERA SVQVSDPSIT
     DAQLVEAVEK GGYGAHVREA AAESTSIHGP DTSAEERAAR DKRDTLIRTV LAAILSAPIF
     LISMIPALQF PGWQWAMLIL ATPVVFYCGA PFHRATWVNI KHGGFTMDTL VTMGTFAAYL
     WSIWALLFGG AGEIGMTMDM SLGAAFSRNQ HGAHEIYFES AAVITTLVLA GRYAQARAIH
     QSSAAIRSLL DLGAKNATIV ELQSDGSTAE VEVPIGAVRV GDVFVVRPGE KVATDGVILE
     GSSAIDRSML TGESIPEDVT PGTEVTGATV NTTGRLLVRA TRVGADTELA HIAKMVEDAQ
     ASKAPVQQLV DKVASIFVPI VIVLAILTLV AWIALGGTTE QAFTAAVAVL IIACPCALGL
     ATPTAIMVGT GRGAELGILI RSASTLESSR DIATIVLDKT GTLTSGAMRV HSVTPAEGWS
     EANIRALAGA AESGSEHPIA RAIVEAAGGS SDALTLEDAR AHVGRGLTAR VSGSLGGITG
     PWEVEITAAS DAGQASAGTE NPTVPSLPAP LAASLREAEQ AGHTTSIVRV NGEIAGLVRV
     SDTVKPEATK VVEEIRALGI EPVMATGDNP AAAEHIAREV GIEKVHASLT PAAKLDLVKS
     LRGEGASVAM VGDGINDTAA LAEADLGFAM GTGTDAAMNS GDIVLTGGDI AQIPTAIRLS
     RASVRTIRWN LFWAFIYNVI AIPLAMLGLL GPVIAAAAMA FSSVFVVSNS LRLKRFQ
//
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