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Database: UniProt
Entry: A0A172U1Q1_9BACT
LinkDB: A0A172U1Q1_9BACT
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ID   A0A172U1Q1_9BACT        Unreviewed;       847 AA.
AC   A0A172U1Q1;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
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=SY85_02755 {ECO:0000313|EMBL:ANE53279.1};
OS   Flavisolibacter tropicus.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Flavisolibacter.
OX   NCBI_TaxID=1492898 {ECO:0000313|EMBL:ANE53279.1, ECO:0000313|Proteomes:UP000077177};
RN   [1] {ECO:0000313|Proteomes:UP000077177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LCS9 {ECO:0000313|Proteomes:UP000077177};
RA   Kim M.K., Srinivasan S., Lee J.-J.;
RT   "Flavisolibacter sp./LCS9/ whole genome sequencing.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ANE53279.1, ECO:0000313|Proteomes:UP000077177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LCS9 {ECO:0000313|EMBL:ANE53279.1,
RC   ECO:0000313|Proteomes:UP000077177};
RX   PubMed=27259556; DOI=10.1099/ijsem.0.001207;
RA   Lee J.J., Kang M.S., Kim G.S., Lee C.S., Lim S., Lee J., Roh S.H., Kang H.,
RA   Ha J.M., Bae S., Jung H.Y., Kim M.K.;
RT   "Flavisolibacter tropicus sp. nov., isolated from tropical soil.";
RL   Int. J. Syst. Evol. Microbiol. 66:3413-3419(2016).
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; CP011390; ANE53279.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A172U1Q1; -.
DR   STRING; 1492898.SY85_02755; -.
DR   KEGG; fla:SY85_02755; -.
DR   PATRIC; fig|1492898.3.peg.603; -.
DR   Proteomes; UP000077177; 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; 3.
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:UP000077177};
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        52..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        75..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        236..254
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        266..289
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        718..742
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        748..769
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        781..801
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        816..839
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..72
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
SQ   SEQUENCE   847 AA;  94932 MW;  F12CC0E1EE02269A CRC64;
     MGLPLNELKT RMGFFREGLT TQEATKRLQQ YGFNEIAKEK PLSALKRLWN HLKNPLVILL
     SVLGVVSWLT SDIRATIVIF VMVLLGIILR YFQEMRADKA AEKLKAMVST HASVRRDNKD
     IEIPLKMLVP GDIIMLGAGD MVPADVRILS AKDLFVNQAA LTGESLLVEK NDKESHSENN
     NPLELLNTCF LGTNVISGSA TALVIHTGDD TYFGNIAYNL AGERQPTSFD KGINRFTWLM
     IRFIFIMVPA VFLINGLSRH NWVEAFLFAL AVAVGLTPEM LPMIISVNLS KGAIAMSRKK
     VIVKRLNSIQ NFGAMDVLCT DKTGTITRGK IVLEQHLDVK GGESQKVLDF GYLNSFYHTG
     LKNIMDDAIL DHEELETALK IKDTYKKIDE IPFDFVRKRM SVVVEDKTGL NMLICKGAVE
     NLLDLCTQVE VGREMKVMKN EDREECLQLV HRLNSNGFRV LAIAYKYIPG GSDEQVYKTA
     DESDLVLLGY LSFFDPPKET ASEALQRLEK LNIEVKILTG DNEAITAYIC KKVGIKTEQV
     LLGPAIENMT EEQLKEAAGN YNVFARLVPT HKKRIIQALQ KSGHVIGFMG DGINDAPALK
     AADIGISVDS AVDVAKESSD IILLETSLLV LEQGVAEGRR VFGNIIKYIE MAASSNFGNM
     FSVVGASAFL PFVPMLPIQI LTNNLLYDFS QTTIPTDNVD KEWLIKPRKW AIGELQRFIL
     FIGPISSIFD YITFFIMWFI FHAKNNEALF HTGWFVESLF TQTLIIHIIR TNKISFIQSR
     ASWQLITSSI IIVFVGAWLT VSPLATTLGF VSLPPLYWSL LVLILFCYII LTQLMKSWLI
     RRYGASR
//
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