ID Q2NJN4_AYWBP Unreviewed; 892 AA.
AC Q2NJN4;
DT 07-FEB-2006, integrated into UniProtKB/TrEMBL.
DT 07-FEB-2006, sequence version 1.
DT 27-MAR-2024, entry version 119.
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=mgtB {ECO:0000313|EMBL:ABC65359.1};
GN OrderedLocusNames=AYWB_242 {ECO:0000313|EMBL:ABC65359.1};
OS Aster yellows witches'-broom phytoplasma (strain AYWB).
OC Bacteria; Mycoplasmatota; Mollicutes; Acholeplasmatales;
OC Acholeplasmataceae; Phytoplasma; 16SrI (Aster yellows group).
OX NCBI_TaxID=322098 {ECO:0000313|EMBL:ABC65359.1, ECO:0000313|Proteomes:UP000001934};
RN [1] {ECO:0000313|EMBL:ABC65359.1, ECO:0000313|Proteomes:UP000001934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AYWB {ECO:0000313|EMBL:ABC65359.1,
RC ECO:0000313|Proteomes:UP000001934};
RX PubMed=16672622; DOI=10.1128/JB.188.10.3682-3696.2006;
RA Bai X., Zhang J., Ewing A., Miller S.A., Jancso Radek A., Shevchenko D.V.,
RA Tsukerman K., Walunas T., Lapidus A., Campbell J.W., Hogenhout S.A.;
RT "Living with genome instability: the adaptation of phytoplasmas to diverse
RT environments of their insect and plant hosts.";
RL J. Bacteriol. 188:3682-3696(2006).
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; CP000061; ABC65359.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2NJN4; -.
DR STRING; 322098.AYWB_242; -.
DR KEGG; ayw:AYWB_242; -.
DR eggNOG; COG0474; Bacteria.
DR HOGENOM; CLU_002360_6_3_14; -.
DR PhylomeDB; Q2NJN4; -.
DR Proteomes; UP000001934; 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; 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; 1.
DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR42861:SF156; CALCIUM-TRANSPORTING ATPASE; 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 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 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 69..90
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 102..121
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 268..286
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 292..319
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 713..734
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 755..778
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 790..809
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 821..842
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 862..880
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 20..93
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 892 AA; 100258 MW; 4894418004F48EAA CRC64;
MFNMKKVNLK RQETIDFLKT MSQKSQEKTL QTLNSSLKGL DQKQVMLHQS LYGKNILSQE
TKTSFTKQLL QIAITPFNIV LLILTLISLF NDVLTPSQEN RSYSTVITTI LMFLGSVIVQ
FSQESKHLKI TSQLKTLVQN TTAVKRNNFK MEIALEEVVR GDIVILSAGD VIPADIKLLE
TKDFFVKTTT FTGESEPVEK MACSFLQSET ILDDPKLVLA GSTVISGYAT GIVLVTGKDT
YLGNISQEIT KKKSLSHLDQ SINTIAKLLM ICICLMAPLV FLFNFYKPQN TFLQSFLFAL
TIAFGLTPKM LPLIVATSFS KGIVALSKRK VIVKNLNAIS SFGAMNILFT DKTGTLTEDQ
IFLENFLDLN GNEDIRVLRH AYLNSFFQTG LKSLIDKAII TKTNNAKTLH PSLQGITAQF
TKIDEIPFDF KRRKMSVVIQ DASQKQQMIT KGAIEEILSI CDHVELEGKV VPLSDQSKQI
VLQQTITYNQ KGYRVVGVAQ KLISNPKQQP CFTPGQIEEK SMVLIGLLTF LDPIKESSTQ
TISSLQQKGI IVKILTGDND ILTKAIAQKL NIQTTYCLQG SVVDNLSDDA LYEASQKTNL
FTKLSPEQKA RIVSVFKQKG NIVAFMGDGI NDASAMKQAN LGICVDSGAE ITKEIADIIL
LEKQLTVLEQ GVLEGRKTYT NALKYIKFTL SSNFANSLSI LLASLCLNFQ PMIVLQVLFL
DLIYDLICFA IPFDNVDDFY LQKPCKWDFA SIKSFMLWFG FCSFLLDFAF LIGMKFLLKN
LSQNDRLFQT SWFIFSMWSQ TLTIFLLRTD KIIAKNNQKN LPSFLIMVCC CLGLIITTFL
PLIPIVSQAL HLDQSIFEKT TIFPFLLFLV VIYSLVMIWA KKIFIQKHKQ LL
//
