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Database: UniProt
Entry: A0A1S2K6C9_9ACTN
LinkDB: A0A1S2K6C9_9ACTN
Original site: A0A1S2K6C9_9ACTN 
ID   A0A1S2K6C9_9ACTN        Unreviewed;       765 AA.
AC   A0A1S2K6C9;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Copper-translocating P-type ATPase {ECO:0000313|EMBL:OII63169.1};
GN   ORFNames=BJP40_25365 {ECO:0000313|EMBL:OII63169.1};
OS   Streptomyces sp. CC53.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1906740 {ECO:0000313|EMBL:OII63169.1, ECO:0000313|Proteomes:UP000179639};
RN   [1] {ECO:0000313|EMBL:OII63169.1, ECO:0000313|Proteomes:UP000179639}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC53 {ECO:0000313|EMBL:OII63169.1,
RC   ECO:0000313|Proteomes:UP000179639};
RA   Cruz-Morales P., Ramos-Aboites H.E., Barona-Gomez F.;
RT   "Functional and evolutionary genomics of ferrioxamines biosynthesis and
RT   transport.";
RL   Submitted (OCT-2016) 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:OII63169.1}.
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DR   EMBL; MKXB01000143; OII63169.1; -; Genomic_DNA.
DR   RefSeq; WP_071280673.1; NZ_MKXB01000143.1.
DR   AlphaFoldDB; A0A1S2K6C9; -.
DR   STRING; 1906740.BJP40_25365; -.
DR   Proteomes; UP000179639; 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; 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; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00403; HMA; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00943; CUATPASE.
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:UP000179639};
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        115..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        138..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        176..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        219..237
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        371..393
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        399..420
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        715..732
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        738..756
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          18..83
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   REGION          79..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   765 AA;  78696 MW;  143FB45AC7152FC6 CRC64;
     MSSHATASTP AAGTGATAEV ELAIGGMTCA SCAARIEKKL NRMDGVEATV NYATEKAKVA
     YRGADVSVQD LIATVEATGY TAREPEPPAP SPTADGGQGD TAEDDPELTA LRQRLVTAVV
     LSVPVIALAM IPPLQFTYWQ WLSLTLAAPV VVYAGWPFHR AAWTNLRHGA ATMDTLISVG
     TSAAFLWSLW ALFFGTAGTP GMSHPFTFAV SRGGGAGNIY LEAAAGVTAF ILAGRYFEAR
     SKRKAGAALR ALLELGAKEV TVLRDGRQQL IPTADLHVGD RFLVRPGEKI ATDGTVVEGS
     SAVDASMLTG ESVPVEVAVG DAVAGATLNA GGRLVVEATR VGADTQLARM AKLVEDAQNG
     KAAAQRLADR ISAVFVPVVI LLALATLGAW LAFGAGLAAA FTAAVAVLII ACPCALGLAT
     PTALMVGTGR GAQLGILIKG PEVLETTRKA DTLVLDKTGT VTTGRMTLLA VHPGASTTEH
     EVLRLAGALE HASEHPVAQA VAAGAAERTG TLPDPEDFVN VPGLGVQGVV DGHAVLVGRE
     KLLAQWAVEL PEDLARAKEA AERSGRTAVT VAWDGEARAV LEVADAVKDT SAEAVRRLRA
     LGLTPILLTG DNRAVAEAVA REVGIDPAHV IAEVLPEGKV DVVKRLQAEG RSVAMVGDGV
     NDAAALAQAD LGLALGTGTD AAMEAGDLTL VRGDLRAAAD AIRLSRRTLA TIKGNLFWAF
     AYNVAALPLA VAGLLNPMIA GAAMAFSSVF VVGNSLRLRG FKAAD
//
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