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
//