ID A0A0J7LU59_9FLAO Unreviewed; 895 AA.
AC A0A0J7LU59;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=ACM44_01725 {ECO:0000313|EMBL:KMQ72485.1};
OS Chryseobacterium koreense CCUG 49689.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=1304281 {ECO:0000313|EMBL:KMQ72485.1, ECO:0000313|Proteomes:UP000035900};
RN [1] {ECO:0000313|EMBL:KMQ72485.1, ECO:0000313|Proteomes:UP000035900}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 49689 {ECO:0000313|EMBL:KMQ72485.1,
RC ECO:0000313|Proteomes:UP000035900};
RX PubMed=15545478; DOI=10.1099/ijs.0.02998-0;
RA Kim M.K., Im W.T., Shin Y.K., Lim J.H., Kim S.H., Lee B.C., Park M.Y.,
RA Lee K.Y., Lee S.T.;
RT "Kaistella koreensis gen. nov., sp. nov., a novel member of the
RT Chryseobacterium-Bergeyella-Riemerella branch.";
RL Int. J. Syst. Evol. Microbiol. 54:2319-2324(2004).
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:KMQ72485.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LFNG01000002; KMQ72485.1; -; Genomic_DNA.
DR RefSeq; WP_048498394.1; NZ_LFNG01000002.1.
DR AlphaFoldDB; A0A0J7LU59; -.
DR STRING; 1304281.ACM44_01725; -.
DR PATRIC; fig|1304281.5.peg.368; -.
DR OrthoDB; 1521937at2; -.
DR Proteomes; UP000035900; Unassembled WGS sequence.
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; 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 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:UP000035900};
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 74..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 108..127
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 270..291
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 303..327
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 764..787
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 829..851
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 863..883
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 25..98
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 895 AA; 99913 MW; 205C4E977E835178 CRC64;
MKLFYKTKII TPKISSGHHV LLLQKISALS PEAAILNMKT SDDGLSEEEA KKRLEEYGPN
EANYQKAPKW YRQLLNAFLN PFTFILMVIA VISYFVDNIM AAANEKDPST VIIISIMVVF
SGLLRFWQEF RSNRAAEQLK KMVTTSTTVK RKNKPPEEIS VTQIVPGDLI KLSAGDMVPA
DCRIIQSKDL FCSEAMLTGE AMPTEKNSTA IPNAAMQIPL MLENLCFMGT NIVSGSATAL
VLNTATQTYF GQISEKISEK RSESEFEKGV NKVSFLLIRF MLVMVPLIFL INGLIKGNWI
EALLFAIAVA VGLIPEMLPM IVTANLSKGS IAMSKKKVIV KHLDAIQNIG AMNILCCDKT
GTITKNEIAL EKHLNADGND DKEVLKWAYL NSYFQTGLRN LMDEAVLKHT EVQDLINIES
DFQKVDEIPF DFERRRMSVI LKMKNGKQLL ICKGAVEEII GLCTKSFDPG PDKELHIEQD
KQIDLDENVK NKILNISKQM NEEGLRVLLI AIREFGENHP TNYSKKDESE LTMTGFIGFL
DPAKPSAGPS IEALHQLGVE VKIITGDNDL VAKKVGKDVG LSTDKIMLGE ELERLSDEEL
KGKLSETVIF AKINPMQKLR IVNLLRKAGN TIGFIGDGIN DAAALKEADV GISVDSAVDI
SKESADIILL EKDLMVLREG VLAGRQTFGN IIKYIKMAAS SNFGNMFSML GASALLPFLP
MLPLQIITQN LLYDFSQSAI PWDKMDQDFL EQPKKWEAGS IQRFMLWIGP ISSIFDYATF
AVMFFIFKAN SPEHQTLFQT GWFVEGLLSQ TLIVHMIRTR KIPFIQSWAS APLTAVTSLI
MLIAIAIPFT PVAASLKMQA LPIAYFPWLA GILLMYSLLT QLVKTWYIKK YNEWL
//
