ID W9BJG1_KLEPN Unreviewed; 902 AA.
AC W9BJG1;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 82.
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 Name=mgtA {ECO:0000313|EMBL:SXU35452.1};
GN ORFNames=BB784_24620 {ECO:0000313|EMBL:APP54918.1}, SAMEA3512100_04240
GN {ECO:0000313|EMBL:SXU35452.1}, SAMEA4873632_04451
GN {ECO:0000313|EMBL:VGL09961.1};
OS Klebsiella pneumoniae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=573 {ECO:0000313|EMBL:SXU35452.1, ECO:0000313|Proteomes:UP000259753};
RN [1] {ECO:0000313|EMBL:APP54918.1, ECO:0000313|Proteomes:UP000184679}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Kp_Goe_827024 {ECO:0000313|EMBL:APP54918.1,
RC ECO:0000313|Proteomes:UP000184679};
RA Bohne W., Bunk B., Overmann J., Gross U., Zautner A.E.;
RT "A nosocomial outbreak of oxa48-expressing Klebsialla pneumoniae in Lower
RT Saxony.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SXU35452.1, ECO:0000313|Proteomes:UP000259753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5012STDY7626430 {ECO:0000313|EMBL:VGL09961.1,
RC ECO:0000313|Proteomes:UP000376235}, and EuSCAPE_DE072
RC {ECO:0000313|EMBL:SXU35452.1, ECO:0000313|Proteomes:UP000259753};
RG Pathogen Informatics;
RL Submitted (AUG-2018) 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; CP018701; APP54918.1; -; Genomic_DNA.
DR EMBL; UKLK01000009; SXU35452.1; -; Genomic_DNA.
DR EMBL; CAAHCC010000010; VGL09961.1; -; Genomic_DNA.
DR RefSeq; WP_009309303.1; NZ_WYAL01000031.1.
DR KEGG; kpnk:BN49_4783; -.
DR Proteomes; UP000184679; Chromosome.
DR Proteomes; UP000259753; Unassembled WGS sequence.
DR Proteomes; UP000376235; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 2.
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; 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 Hydrolase {ECO:0000313|EMBL:SXU35452.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
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 122..141
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 295..313
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 319..346
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 772..795
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 837..861
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 873..895
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 48..121
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 902 AA; 99909 MW; 7D0AA19EF6CC89BE CRC64;
MLKNYTRQLF AQLSRHLPRR LVQRDPLPDA RHLASGPIPE SLGQHCLNVA AMDDQEIWRA
FDSHPEGLNE GEVAAKILKH GDNQIPAQKP SPWWVHLWTC YRNPFNLLLT VLGIVSYSTE
DLFAAGVIAL MVGISTLLNF IQEARSTKAA DALKAMVSNT ATVLRVVNEQ GESRWLELPI
DQLVPGDIIR LSAGDMIPAD LRILQARDLF VAQASLTGES LPVEKVARSR DPLQQNPLEC
DTLCFMGTNV VSGSAQAIVF ATGGRTWFGQ LAGRVSEQES EPNAFQKGIS RVSMLLIRFM
LVMAPVVLLI NGYTKGDWWE AALFALSVAV GLTPEMLPMI VTSTLARGAV KLSKQKVIVK
HLDAIQNFGA MDILCTDKTG TLTQDKIVLE NHTDVSGKVC ERVLHAAWLN SHYQTGLKNL
LDTAVLDGVE LDAARGLAER WQKVDEIPFD FERRRMSVVV KEDDAAHQLI CKGALQEILN
VSTQVRYNGD IVPLDDTMLR RIRRVTDTLN RQGLRVVAVA TKYLPAREGD YQRADESDLI
LEGYIAFLDP PKETTAPALK ALKASGITVK ILTGDSELVA AKVCHEVGLD AGEVVIGSQI
EAMSDDELAA LAKRTTLFAR LAPLHKERIV TLLKREGHVV GFMGDGINDA PALRAADIGI
SVDGAVDIAR EAADIILLEK SLMVLEEGVI EGRRTFANML KYIKMTASSN FGNVFSVLVA
SAFLPFLPML PLHLLIQNLL YDVSQVAIPF DNVDDEQIRK PQRWNPADLG RFMVFFGPIS
SIFDILTFGL MWWVFHANTV EMQTLFQSGW FIEGLLSQTL IVHMIRTRRI PFVQSRAAWP
LFAMTLVVMA VGIALPFSPL ASYLQLQALP LSYFPWLVAI LAGYMVLTQA VKGFYSRRYG
WQ
//
