ID S5LW71_9MOLU Unreviewed; 896 AA.
AC S5LW71;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
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:AGR40851.1};
GN ORFNames=STAIW_v1c01740 {ECO:0000313|EMBL:AGR40851.1};
OS Spiroplasma taiwanense CT-1.
OC Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC Spiroplasma.
OX NCBI_TaxID=1276220 {ECO:0000313|EMBL:AGR40851.1, ECO:0000313|Proteomes:UP000014984};
RN [1] {ECO:0000313|EMBL:AGR40851.1, ECO:0000313|Proteomes:UP000014984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT-1 {ECO:0000313|EMBL:AGR40851.1};
RX PubMed=23873917; DOI=10.1093/gbe/evt108;
RA Lo W.S., Ku C., Chen L.L., Chang T.H., Kuo C.H.;
RT "Comparison of metabolic capacities and inference of gene content evolution
RT in mosquito-associated Spiroplasma diminutum and S. taiwanense.";
RL Genome Biol. Evol. 5:1512-1523(2013).
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}.
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DR EMBL; CP005074; AGR40851.1; -; Genomic_DNA.
DR RefSeq; WP_020833990.1; NC_021846.1.
DR AlphaFoldDB; S5LW71; -.
DR STRING; 1276220.STAIW_v1c01740; -.
DR KEGG; stai:STAIW_v1c01740; -.
DR PATRIC; fig|1276220.3.peg.174; -.
DR eggNOG; COG0474; Bacteria.
DR HOGENOM; CLU_002360_6_3_14; -.
DR OrthoDB; 9813266at2; -.
DR Proteomes; UP000014984; 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 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; 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 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000014984};
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 66..88
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 100..119
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 277..298
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 310..334
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 682..706
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 750..775
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 834..852
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 864..884
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 19..91
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 896 AA; 101745 MW; A9AE8883FB9BBA8A CRC64;
MRANQNKNNK NNKNTRLIEY IDLNQQQILK KLEISQFGLT PDEVITQRER FGDNNLKAHK
MNVLSAFIKS FFSPFNLILI IIDTFSFYTY ATEGKNPFDL FGALLVLIMI LLSGTIYFVQ
EIRSFLVIKK MKYENKQMCK VIRDVNFKIN DIDNANSIKL IKEYISLENS ELVQGDLIYL
SNGDLIPADI KVVWSNNLYL NQSSLTGESF PVQKKITNAK ENYLEFENIC YMGTEVVSGS
ALGIVLSTGQ NTYFSEMNDK VTEKRPVNSF EKGIKRITLL LISFMLATTP IVFLVFGLRT
DDFDHRWLSA ALFSISIAVG LTPEMLPIIV TANLSRGYSK IKKEKVLVKN LNAVQNMGAI
DILCTDKTGT ITSGEINLDK VFDIKNQKNP YIEEILYLNS YFQTGFQNPI DQAVLLSKNI
KHIDVEEYKK EWEVPFDFKR KILSVILSKN EQKQIFTKGA IEEILKICNR IYINGEIKEL
TNEYKEKIIN KSSEFNNEGF RVIGIAHNSL EDEDIEEDLI FYGFATFFDQ PKKTSKAIIK
QLLDRGITTK ILTGDDEVIT RAICKKVDFK IEKLYTGKEI EAMDEQQLAK AVIRANVFVK
LSPMHKSLII KTLKSQQHVV GFMGDGINDA PVLRESDVAI SFKEASNIAQ EAADLILLEE
SLLPISAAVY EGRVSLANIL KYIKVTVASN FGNVLSVLIA LFLTLAEPMQ PLHLLAQNLL
YDIVMFAFIF DKVDKNFTDK PRPLKTKNII WFTIINGPVS SIFDIVTFLV LLYAFRQQIG
LEPGISANIE IPKEAIAKFN ASWFVVGLMT QTAVMQMYRT EKIPFLQSNG SWQVNLSTVF
VCLMAIIIPF TPINKVLAMQ TPPWAFLGVA ISFVLAYVCL AQVVKMGYIK MFKEWL
//
