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Database: UniProt
Entry: A0A089WI59_9PSED
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ID   A0A089WI59_9PSED        Unreviewed;       897 AA.
AC   A0A089WI59;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
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   ORFNames=LK03_06780 {ECO:0000313|EMBL:AIR88990.1};
OS   Pseudomonas cremoricolorata.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=157783 {ECO:0000313|EMBL:AIR88990.1, ECO:0000313|Proteomes:UP000029493};
RN   [1] {ECO:0000313|EMBL:AIR88990.1, ECO:0000313|Proteomes:UP000029493}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ND07 {ECO:0000313|EMBL:AIR88990.1,
RC   ECO:0000313|Proteomes:UP000029493};
RA   Chan K.-G.;
RL   Submitted (SEP-2014) 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}.
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DR   EMBL; CP009455; AIR88990.1; -; Genomic_DNA.
DR   RefSeq; WP_038411617.1; NZ_CP009455.1.
DR   AlphaFoldDB; A0A089WI59; -.
DR   STRING; 157783.LK03_06780; -.
DR   KEGG; psw:LK03_06780; -.
DR   eggNOG; COG0474; Bacteria.
DR   OrthoDB; 9814270at2; -.
DR   Proteomes; UP000029493; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000029493};
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        75..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        105..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        281..302
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        314..338
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        766..789
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        831..851
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        867..885
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          18..91
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
SQ   SEQUENCE   897 AA;  98692 MW;  FA356F3BBBFB0BED CRC64;
     MTVKDRNTNQ KLSMRAAREA RNGLQVTFAN LDTAEHGLTE REAGKRLERD GRNEVSHDKP
     PSASLQFLKA LNNPFIYILL ILAAISFITD YWLPVRADDL EEADLTKVII IMTMVNLSGL
     LRFWQEYRSN KAAEALKAMV RSTASVLRRE KQGEAPRLRE VAMGELVAGD IVQLSAGDMI
     PADVRLIESR DLFISQAVLT GEALPVEKYD TLGDVAQKCA ADSAELSQDL LDLPNTCFMG
     TNVVSGRARA VVVATGSRTY FGSLAKSISG SRSQTAFDRG VNSVSALLIR FMLVMVPVVF
     MINGLVKGDW GDAFLFALAV AVGLTPEMLP MIVSANLAKS AVAMAKQKVV VKRLNAIQNL
     GSMNVLCTDK TGTLTEDRIV LADHVDLDGQ RAPHLLELAW LNSHHQSGVR NLMDQAIITC
     ATNTVDFHPP YAYAKVDELP FDFVRRRLSV VLDNGNGQHL VVSKGAVEEM LAVATHVEYA
     GGALPLDEDR RQALLAQASA YNERGLRVLL LATRIVNGTR CKRQYAVEDE RELVIRGLLT
     FLDPPKASAS QALAALREQG VTVKVLTGDN PQVASTICRQ VGLEPGQPIL GHDIDSLGEA
     ELKQVVEQRT LFAKLTPLQK SRVVKALQNN GHTVGFLGDG INDAPALRDA DVGISVDSGT
     DIAKESADII LLEKDLLVLE QGVLKGRETF GNIMKYLCMT ASSNFGNVFS VLVASAFIPF
     MPMLALHLLL QNLMYDFSQL SLPWDKLDKE FLSQPRRWDS SNIGRFMLWI GPTSSIFDIT
     TFALMWFVFA ANSVEMQALF QSGWFIEGLL SQTLVVHMLR TRKVPFFQST AAWPVILATG
     VVMCLGIYIP FSPLGAMVGL VPLPWEYFPW LVATLLGYCL VAQGMKTLYI RRFGQWF
//
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