ID K1SC83_9ZZZZ Unreviewed; 874 AA.
AC K1SC83;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, 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=OBE_17141 {ECO:0000313|EMBL:EKC44986.1};
OS human gut metagenome.
OC unclassified sequences; metagenomes; organismal metagenomes.
OX NCBI_TaxID=408170 {ECO:0000313|EMBL:EKC44986.1};
RN [1] {ECO:0000313|EMBL:EKC44986.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=22891823; DOI=10.1111/j.1462-2920.2012.02845.x;
RA Ferrer M., Ruiz A., Lanza F., Haange S.B., Oberbach A., Till H.,
RA Bargiela R., Campoy C., Segura M.T., Richter M., von Bergen M., Seifert J.,
RA Suarez A.;
RT "Microbiota from the distal guts of lean and obese adolescents exhibit
RT partial functional redundancy besides clear differences in community
RT structure.";
RL Environ. Microbiol. 15:211-226(2013).
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}.
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:EKC44986.1}.
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DR EMBL; AJWZ01011491; EKC44986.1; -; Genomic_DNA.
DR AlphaFoldDB; K1SC83; -.
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 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 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 84..117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 292..316
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 742..765
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 777..795
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 811..832
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 844..862
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 30..100
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 874 AA; 98977 MW; 59E9F9A246ECAB4F CRC64;
MIRIFDIKNS KNDLKHNDNE IFKNYLTESK ENTYNSLQKY KSTLNGLSEK EVKKRLNENG
KNVVIKDEHK GPLYFLLESF KDEFIIILLF LSLINLFLGD TLGSIIIIVI AFISALIRFF
QDYSVYKFNK KLQSKIYSTV IVLRNNEEME IKVEDVVVGD IVKLNAGTIM PADLKIIDCK
DLFINQSVFT GESVLIEKKQ LSSNNPKEIF DIENICLMGT SVVSGRGSGL VISTGFDSYL
GKVGSEIKDK KEETNFDKGI KSISNLLIKY MAIVCLVVIV IDGILKQNMG EALLFALSVA
VGITPSMLPM ILNVNLTKGS KSLAKKKTLV KKIESIQNLG AIDILCTDKT GTLTENEITL
QKYIDALGKE NEDILEYAFL NSYYSTGIKN LVDRAIISYG KQNKIDEKVK IYEKVDEIPF
DYNRKKQSIV VKHKNTYRMI TKGALEEVIK DCNMVHTNDK NEVITEKIKK VIKSKAIELA
NDGMQVIALA EKNSYPGINS FNTDYEKDMT FVGFVAFLDP AKKDVKKTLS NLYKIGIKTK
ILTGDNPYAT KNICNMVGLN GNDILLGSDI DKMTDEQLSS RIEEVDVFAR MNPLQKERIV
SLYRKNNHVV GYMGDGVNDA PSLSEADVGI SVNTATSIAK EASDIIILKQ SLKVIYDGVL
EGRKVYGNII KYMKMALSAD FGDVFSIMIS SIFIPFLPLL PIQMLLQDFI YDFSQIGIPY
DNVDESFLIE PKKWDTKGIS RFMKVMGITS SLIDIISFII FWFIFKYNSV DKQAYFQTAW
FVTCLTTELM IIYNVRTAKR PFIESNASSK LNILTIFSLA LTIITPIILH NIKTFHFVIL
PTSFYFYLIG LVLLYFIIVS IIKRIYIAKY DEWL
//
