ID A0A0G3ACD5_9ACTN Unreviewed; 924 AA.
AC A0A0G3ACD5;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Magnesium ABC transporter ATPase {ECO:0000313|EMBL:AKJ09977.1};
GN ORFNames=ABB07_08065 {ECO:0000313|EMBL:AKJ09977.1};
OS Streptomyces incarnatus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=665007 {ECO:0000313|EMBL:AKJ09977.1, ECO:0000313|Proteomes:UP000035366};
RN [1] {ECO:0000313|EMBL:AKJ09977.1, ECO:0000313|Proteomes:UP000035366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL8089 {ECO:0000313|Proteomes:UP000035366};
RX PubMed=26159526;
RA Oshima K., Hattori M., Shimizu H., Fukuda K., Nemoto M., Inagaki K.,
RA Tamura T.;
RT "Draft Genome Sequence of Streptomyces incarnatus NRRL8089, which Produces
RT the Nucleoside Antibiotic Sinefungin.";
RL Genome Announc. 3:e00715-e00715(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00001836};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP011497; AKJ09977.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G3ACD5; -.
DR STRING; 665007.ABB07_08065; -.
DR PATRIC; fig|665007.5.peg.1766; -.
DR Proteomes; UP000035366; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
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; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR42861:SF156; CALCIUM-TRANSPORTING ATPASE; 1.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF00122; E1-E2_ATPase; 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 SMART; SM00831; Cation_ATPase_N; 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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 73..106
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 257..278
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 721..746
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 758..778
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 864..883
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 895..914
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 16..89
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 924 AA; 95951 MW; 10B26AA0A554EB02 CRC64;
MASEAPTGPV GGPGTGPASG TSLQVLRRLD TGPRGLTDAE AAARLATHGE NAPPRPRTPS
ALRRCLRGLR DPFTAVLLTL GLVSAFVASW GTATVILALV AVSCALRAAG ERRADRSLAS
LRELVAGTAS VLRRADGTAA PRAHEVPVAD LVPGDVVRLG PGDLVPADVR LLRARGLTVS
EAALTGESAP VAKAAAEPPE PPGESTLCFQ GSAVVAGSAT AVVVATGART RFAAAQRAPR
AREPSAFDRS VHGIARVLVR FMLLTPPLVL MAGAVLRGQG LQTLPFAVSV AVGLTPEMLP
VIVTTCLARS AALLARTRRV VVRRLPALHD LGAIDVLCVD KTGTLTQDRP VAARSLGPDG
RDDPEVLRWA AAGAWWTLNL AELPAPDALD AALLDVAGSA GEEYDGLAAL PVAPGRRLAT
AVVAGRLGHH LLITKGAAED VLARCALPDA ERQRLLALAA REAETGQRVL AVATAERPAR
TRPYTPADER GLTFRGLVTF RDELAPGAAE SLRTLASLGV GVHILTGDHP ATAARVCREA
GLEPGEVRTA QGGAGEGPGP GRALGTTTVV ARCTPEDKAR VVAGLRAAGH TVGFLGDGVN
DVAALLAADV GIAPRGAVAV ARESADVVLA EKDLTAIGHA VTAGRRSSAN IAAYLRVTLS
SNLGNVLAML AAGLLLPFLP MLPVQVLAQN LCFDAAQLAF AHDRPAPGEL RRPTVLRPPA
FLRFITGFGV LNAFADLATF GVLTLALNGP DALHDEAVFH SAWFTENLLT QALVMLLLRD
GRRLARDSRI LVRDGRRLAC DGRRRACGGW WRLACGGWWP LARGGRRLMC DGWRRTRSGR
RLTSGGRLLA SGRRRLVSGG RSGPVGWAAA FLAAVGIAVP PSPLGAALGM TALPAPYHLL
LAAVLGLYAV ALTVTTKRHA RQRP
//
