ID A0A5R8QFK6_9FIRM Unreviewed; 893 AA.
AC A0A5R8QFK6;
DT 26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2020, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Magnesium-transporting ATPase, P-type 1 {ECO:0000256|ARBA:ARBA00013555};
DE EC=7.2.2.14 {ECO:0000256|ARBA:ARBA00012786};
DE AltName: Full=Mg(2+) transport ATPase, P-type 1 {ECO:0000256|ARBA:ARBA00029806};
GN Name=mgtA {ECO:0000313|EMBL:TLG76540.1};
GN ORFNames=FEZ08_02685 {ECO:0000313|EMBL:TLG76540.1};
OS Culicoidibacter larvae.
OC Bacteria; Bacillota; Culicoidibacteria; Culicoidibacterales;
OC Culicoidibacteraceae; Culicoidibacter.
OX NCBI_TaxID=2579976 {ECO:0000313|EMBL:TLG76540.1, ECO:0000313|Proteomes:UP000306912};
RN [1] {ECO:0000313|EMBL:TLG76540.1, ECO:0000313|Proteomes:UP000306912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CS-1 {ECO:0000313|EMBL:TLG76540.1,
RC ECO:0000313|Proteomes:UP000306912};
RA Neupane S., Ghosh A., Gunther S., Martin K., Zurek L.;
RT "Culicoidintestinum kansasii gen. nov., sp. nov. from the gastrointestinal
RT tract of the biting midge, Culicoides sonorensis.";
RL Submitted (MAY-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Mediates magnesium influx to the cytosol.
CC {ECO:0000256|ARBA:ARBA00003954}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + Mg(2+)(out) = ADP + H(+) + Mg(2+)(in) + phosphate;
CC Xref=Rhea:RHEA:10260, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18420, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; EC=7.2.2.14;
CC Evidence={ECO:0000256|ARBA:ARBA00001857};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIIB subfamily. {ECO:0000256|ARBA:ARBA00008746}.
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:TLG76540.1}.
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DR EMBL; VBWP01000002; TLG76540.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5R8QFK6; -.
DR InParanoid; A0A5R8QFK6; -.
DR OrthoDB; 9760364at2; -.
DR Proteomes; UP000306912; Unassembled WGS sequence.
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 GO; GO:0015444; F:P-type magnesium transporter activity; IEA:UniProtKB-EC.
DR CDD; cd02077; P-type_ATPase_Mg; 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; 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; IPR006415; P-type_ATPase_IIIB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01524; ATPase-IIIB_Mg; 1.
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; PR01836; MGATPASE.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 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 SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022519};
KW Hydrolase {ECO:0000313|EMBL:TLG76540.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000306912};
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 70..95
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 107..126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 273..291
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 297..324
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 679..701
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 749..777
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 789..815
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 827..847
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 862..881
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 22..97
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 893 AA; 98740 MW; D2A26CC236613F13 CRC64;
MSRKADIENK ERQLNQSAMA QLFHAASADS EALLTEYQNS ESGFDDARVL AMRQKYGENR
LTHQRKVPTI VQFLLAFTDP FTIVLFVLAI ISFVSNVLLA PAGQQDPSTV IIILVLIFIS
GTLRFVQQYR SKKSADSLNE MVKTKIDVMR NGKVTEVPIT EIVVGDLVVL SAGDMIPADV
RLISVKDLFV SQAPLTGEST PVEKYAATDS NKNDDVLDLS NVAFMGSNVI SGSATSLVVN
IGDTTMFGAV AQDIAEKPPL TSFDKGINSV SWLLIRLMLV MVPIVFVLNG IHSNDWLNAF
LFALSVAVGL TPAMLPTIVT TNLAKGAVML SKKKVIVKNI DAIQNFGGMD VLCTDKTGTI
TQDKVVLMHA YDVNGDESDR VLEYGYLNSN FQTGLKNLMD VAIIDYAQEQ DKVEQYKEFV
KVDEIPFDFT RRRMSVVVKD SQQRILITKG AIEEMLSVCT LVESEGKTVN LTDELRQQIL
AQVVKYNADG LRVLGLAYKN EPALEDTFSV QDESEMVLLG YLSFLDPPKD SAKTAIASLK
QYGVQVKILT GDNDGVTKTV CHEVGLNVDR ILLGSDIARM SKEELDKATE TVDVFAKLSP
TQKVEVVESL RRNKHVVGFM GDGINDAAAI KQADVGISVD TAVDIAKEAA PIILLEKNLM
VLKDGVIEGR KTYGNIIKYI KMTLSSNFGN IFSIVIASIF LPFLPMLPIQ ILVLNLIYDI
SCTAIPWDNV DVEFLVKPRD WNAKSIKSYM VWLGPTSSIF DITTFIMLFF VLCPLFVGGS
YSSINSEQQL LFAAFFHTGW FVESLWTQTL VIHMIRTPKI PFIQSRASLP MFVFTTLGIL
IGTVLPYTEI GAILKMEPLP AIYYALLVGT ILLYIVLVTV VKKLYVKKYK ELL
//
