ID A0A1H5PWK5_9ACTN Unreviewed; 776 AA.
AC A0A1H5PWK5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=ATPase, P-type (Transporting), HAD superfamily, subfamily IC/heavy metal translocating P-type ATPase {ECO:0000313|EMBL:SEF17578.1};
GN ORFNames=SAMN05216533_8405 {ECO:0000313|EMBL:SEF17578.1};
OS Streptomyces sp. Ag109_O5-10.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1855349 {ECO:0000313|EMBL:SEF17578.1, ECO:0000313|Proteomes:UP000198812};
RN [1] {ECO:0000313|EMBL:SEF17578.1, ECO:0000313|Proteomes:UP000198812}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ag109_O5-10 {ECO:0000313|EMBL:SEF17578.1,
RC ECO:0000313|Proteomes:UP000198812};
RA de Groot N.N.;
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}.
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DR EMBL; FNTQ01000001; SEF17578.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H5PWK5; -.
DR STRING; 1855349.SAMN05216533_8405; -.
DR OrthoDB; 7059309at2; -.
DR Proteomes; UP000198812; 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; cd12108; Hr-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; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR Gene3D; 1.20.120.520; nmb1532 protein domain 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; IPR012312; Hemerythrin-like.
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; 1.
DR PANTHER; PTHR48085; CADMIUM/ZINC-TRANSPORTING ATPASE HMA2-RELATED; 1.
DR PANTHER; PTHR48085:SF5; CADMIUM_ZINC-TRANSPORTING ATPASE HMA2; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF01814; Hemerythrin; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 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 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:UP000198812};
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 25..44
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 51..69
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 81..109
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 246..265
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 271..292
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 638..774
FT /note="Hemerythrin-like"
FT /evidence="ECO:0000259|Pfam:PF01814"
SQ SEQUENCE 776 AA; 80695 MW; 161DC5634A28512B CRC64;
MTHRTTTAQL RRLTSAIGSP RLEPVLLAVT AAALAAGGIA WLTGAGDLAD LCWGLGTLSA
VVPALAWVLT ALWRGHAGVD LIAVLALGGT LAVHEYLAGA LIALMLATGR TLEAAAQRRA
SHDLRALLEH APRSARRRTD AGVASVPLAE VAVGDLLVVG PGEVVPVDGR VEGDAAVLDE
SVLTGEALQV ERTRDETVRS GVVNAGGAFE LRATATEQGS TYAGIVRLAR QAGAESAPVV
RLADRYAAWF LPLSLVVAGL AWLISGSAVR AVAVLVVATP CPLLLAAPVA IVSGLSRASH
LGVVIRDGGA LENLGRARTL LLDKTGTLTR GRPRVLDVIA APDVKPAEVL RLAASLDQYS
PHVLAQAIVD TARERGLVLS VPTDVTEEPG RGATGNVEGH QVFVGRTGAA TARPGWAKAV
DNRALLDGAA VAWLTVDGQP AGAVLLRDPL RHDAPRTLRH LRAAGIERLL MLTGDRAAPA
HEVAAVLGLD DVRAQLGPAD KVAAVRAERE RAVTVMVGDG VNDAPALAAA DIGVAMGARG
STASSEAADI VLTTDRVDRL ADAVTIAQRS RHIAVQSALG GMLMSLAAMA AAAAGLLPPA
AGALLQEGID VAVILNALRA LRVGRAAHPA LTPAAEALIH RFAAEHDDLQ DVLESVRDAA
DRLSDSSGPA SLAAVEETHR LLTERLLPHE YAEEHELYPA LAPTLGGPEA TATMSRAHTE
IERLSRRIAT HLQLAEADGR LSAEQLDDLR SCLYGLNTVL RLHFTQEEEN YFSLAP
//
