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Database: UniProt
Entry: V6KQS2_STRRC
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Original site: V6KQS2_STRRC 
ID   V6KQS2_STRRC            Unreviewed;       864 AA.
AC   V6KQS2;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   24-JAN-2024, entry version 42.
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=M878_10250 {ECO:0000313|EMBL:EST34368.1};
OS   Streptomyces roseochromogenus subsp. oscitans DS 12.976.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1352936 {ECO:0000313|EMBL:EST34368.1, ECO:0000313|Proteomes:UP000017984};
RN   [1] {ECO:0000313|EMBL:EST34368.1, ECO:0000313|Proteomes:UP000017984}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS 12.976 {ECO:0000313|EMBL:EST34368.1,
RC   ECO:0000313|Proteomes:UP000017984};
RX   PubMed=24407645;
RA   Ruckert C., Kalinowski J., Heide L., Apel A.K.;
RT   "Draft Genome Sequence of Streptomyces roseochromogenes subsp. oscitans DS
RT   12.976, Producer of the Aminocoumarin Antibiotic Clorobiocin.";
RL   Genome Announc. 2:e01147-e01113(2014).
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000256|ARBA:ARBA00001836};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004429}. Cell membrane
CC       {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004651}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IIIB subfamily. {ECO:0000256|ARBA:ARBA00008746}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EST34368.1}.
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DR   EMBL; AWQX01000081; EST34368.1; -; Genomic_DNA.
DR   AlphaFoldDB; V6KQS2; -.
DR   STRING; 1352936.M878_10250; -.
DR   PATRIC; fig|1352936.5.peg.2184; -.
DR   HOGENOM; CLU_002360_6_3_11; -.
DR   Proteomes; UP000017984; 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:SF31; PLASMA MEMBRANE ATPASE-RELATED; 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   SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 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:UP000017984};
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        38..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        62..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        224..244
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        250..276
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        692..714
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        726..743
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        755..774
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        780..803
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..58
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          837..864
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   864 AA;  92525 MW;  55B84DFAB6FE149A CRC64;
     MTGDGLSSDE AEQRLRRWGP NAVHSHRARA WLVVWHQLRS PLLGLLLAAA VISYFAGERS
     DALIIGVIVA LSVGLGFLNE YRAEKTAQSL HAKIRHRAVV LRDGRPQEVE VTRLVPGDVV
     ELRLGDIVPA DLRLLQATGL ECSESVLTGE SLPVAKDTAP VPAGTALAEL SGCALMGTVV
     HSGSGRGVVV ATGAEAEFGK IAAGLSGHQL ETEFQVGLRR FSMLLVYVAG ALTTSIFVIN
     VALHKPLIDA LLFSLAIAVG ITPQLLPAVV STSLAAGSRR MSRRKVLVKR LVCIEDLGDV
     DVLFTDKTGT LTHGRIDFMR AVPVGGTSPE EALHLGLLCT ETQVDDQGRP VGGNPLDEAL
     WDSPAAFQRS ALCGFKRIGV LPFDHDRRMV SVMVTDPDGA TTLITKGAPE AVLERCVEVP
     EAARQALDAE FAAANRVVAV ATRPAQATPT LTAADEHDLR LAGLLVFLDP PKPDAAEALG
     RLDALGITVK IVTGDNPAVA AKVCHDLGLN DVGILTGTDL DTMDDEQLTA ALRHTTVFAR
     VSPEHKARIV RSQRRTGGDV AFLGDGVNDA LALHAADVGI SVDSATDVAK DAADVILLEK
     DLGVLADGVA EGRRIFANTI KYVLMGTSSN FGNMFSAAGA SLFLPFLPML PSQILLNNLL
     YDSSQLTIPT DEVDEEQVRR PAHWDIAFIR RFMVCFGPIS SLFDFVTFAV MLWVFHAGPA
     QFHTGWFVES LATQTLVIFA IRTRRIPFWR SHPSLPLAST ALGVVALGTV LPATPLAHVL
     GFRLLPTGFF AAVAAMVAVY LVLVEIGKRI FYRTARAPAR PRPALGHRHL RRRAARFSTT
     TRLRQPRSIG RLPASRPHTT GGVG
//
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