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Database: UniProt
Entry: W0ABC7_9SPHN
LinkDB: W0ABC7_9SPHN
Original site: W0ABC7_9SPHN 
ID   W0ABC7_9SPHN            Unreviewed;       844 AA.
AC   W0ABC7;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-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=NX02_09435 {ECO:0000313|EMBL:AHE53608.1};
OS   Sphingomonas sanxanigenens DSM 19645 = NX02.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1123269 {ECO:0000313|EMBL:AHE53608.1, ECO:0000313|Proteomes:UP000018851};
RN   [1] {ECO:0000313|EMBL:AHE53608.1, ECO:0000313|Proteomes:UP000018851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NX02 {ECO:0000313|EMBL:AHE53608.1,
RC   ECO:0000313|Proteomes:UP000018851};
RA   Ma T., Huang H., Wu M., Li X., Li G.;
RT   "Completed genome of Sphingomonas sanxanigenens NX02.";
RL   Submitted (JUL-2013) 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; CP006644; AHE53608.1; -; Genomic_DNA.
DR   RefSeq; WP_025291856.1; NZ_CP006644.1.
DR   AlphaFoldDB; W0ABC7; -.
DR   STRING; 1123269.NX02_09435; -.
DR   KEGG; ssan:NX02_09435; -.
DR   PATRIC; fig|1123269.5.peg.1847; -.
DR   eggNOG; COG0474; Bacteria.
DR   HOGENOM; CLU_002360_6_3_5; -.
DR   OrthoDB; 391538at2; -.
DR   Proteomes; UP000018851; 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   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; PF13246; Cation_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:UP000018851};
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        55..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        80..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        245..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        271..296
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        714..744
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        779..798
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        804..827
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          6..79
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
SQ   SEQUENCE   844 AA;  90082 MW;  4D05A71BB2C5D751 CRC64;
     MTDPQAFWQA TPDDSLRTLA ATRDGLSSDE AAARLERDGL NEISAAKQRH LLLDLLRRLG
     NPLIAILLVA AGIAGATGDM ASFAIIFIVV VLSTALDLVQ EHRAEATAEA LKQAIALHAT
     VLRDGKPIEL PVRELVAGDI VMLAAGDLVP ADGIVLAANG AQVNEALLTG EPYPVEKQIE
     PVMTAETPAD ARNALFHGTS LIGGTATMLV VQTGLRTRFG AIARSLAGKQ PATAFEHGIH
     KLGTLIVRLT IFLVLFVLLA HLALGRPPLQ SFLFAMALAV GLTPELLPMI MTVALGRGAQ
     RMAKAKVVVK RLSAIHDLGQ MDILCTDKTG TLTEARITLV GHPGIDGEDD ERVAELAAVN
     ARFETGLKSP LDQALVLHMT GRSLEDWRKL DERPFDFERR RVAVLAEQGS ERIEIVKGAP
     ETLLALCTRA QDRSGALLPL DDGLRARLCA LRDDRAAQGL RLLAIAWKPA AGQERIDAHG
     EDELVFAGYC VFVDPPKPSA TTAVARLEAA GIRIKVISGD AAPVIQHLVA ALALPVEGIL
     TGEEIAKLND SALAARVEQV DLFARVTPDQ KTRIVRALRA RGHTVGFIGD GINDAPAIRA
     ADVGLSVDGA TDVAREAADM ILLAPDLGVL ADGVAEGRRT YANIMKYVRM GTSSNFGNML
     TMAVASLFLP FLPLTPVQVL LNNLLYDLSE IGIPFDTADS DDLARPQGWD MRGLVRFTAI
     MGPLSSLFDL ATFALLLGVF HVGIPEFRTA WFMESMLTQI LVVFVIRTSR PAWSSRPHIV
     LTVTALAGLA AALLLPLLPS AGLLGFTMPG GTIFGAIALL VVGYLVSAEC LKRYALRPVK
     SAHR
//
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