ID E3GCH7_ENTLS Unreviewed; 902 AA.
AC E3GCH7;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, 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 OrderedLocusNames=Entcl_3909 {ECO:0000313|EMBL:ADO50148.1};
OS Enterobacter lignolyticus (strain SCF1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Pluralibacter.
OX NCBI_TaxID=701347 {ECO:0000313|EMBL:ADO50148.1, ECO:0000313|Proteomes:UP000006872};
RN [1] {ECO:0000313|Proteomes:UP000006872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCF1 {ECO:0000313|Proteomes:UP000006872};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N.,
RA Mikhailova N., DeAngelis K., Arkin A.P., Chivian D., Edwards B., Woo H.,
RA Hazen T.C., Woyke T.;
RT "Complete sequence of Enterobacter cloacae SCF1.";
RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADO50148.1, ECO:0000313|Proteomes:UP000006872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCF1 {ECO:0000313|EMBL:ADO50148.1,
RC ECO:0000313|Proteomes:UP000006872};
RX PubMed=22180812; DOI=10.4056/sigs.2104875;
RA Deangelis K.M., D'Haeseleer P., Chivian D., Fortney J.L., Khudyakov J.,
RA Simmons B., Woo H., Arkin A.P., Davenport K.W., Goodwin L., Chen A.,
RA Ivanova N., Kyrpides N.C., Mavromatis K., Woyke T., Hazen T.C.;
RT "Complete genome sequence of "Enterobacter lignolyticus" SCF1.";
RL Stand. Genomic Sci. 5:69-85(2011).
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; CP002272; ADO50148.1; -; Genomic_DNA.
DR RefSeq; WP_013367870.1; NC_014618.1.
DR AlphaFoldDB; E3GCH7; -.
DR STRING; 701347.Entcl_3909; -.
DR KEGG; esc:Entcl_3909; -.
DR eggNOG; COG0474; Bacteria.
DR HOGENOM; CLU_002360_6_3_6; -.
DR Proteomes; UP000006872; 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: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; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000006872};
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 123..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; 100198 MW; EA272EFE81FE660B CRC64;
MLKNMTRQLL DQLSRHLPRR LVQRDPMPDR KVLAGTPIPD TLSKQCLDAA AMDENEIWRA
FNSHPEGLNA ADVEENRTRH GENVIPAQKP SPWWIHLWSC YRNPFNLLLT VLGIISYSTE
DLFAAGVIAL MVGISTLLNF IQEARSTKAA DALKAMVSNT ATVLRVINEQ GESRWLEIPI
DRLVQGDIVK LSAGDMIPAD LRVFQARDLF VAQASLTGES LPVEKVARSR DPQQSNPLES
DTLCFMGTNV VSGSAQAIVF ATGGNTWFGQ LAGRVSEQES EPNAFQKGIS RVSMLLIRFM
LVMAPVVLLI NGYTKGDWWE AALFALSVAV GLTPEMLPMI VTSTLARGAV KLSKQKVIVK
HLDAIQNFGA MDILCTDKTG TLTQDKIVLE NHTDVSGRTS DRVLHSAWLN SHYQTGLKNL
LDTAVLEGVD EESARALSER WLKIDEIPFD FERRRMSVVV AEQGDVHQLI CKGALQEILN
VSTQVRFNGD IVPLDDTMLR RIRRVTDNLN RQGLRVVAVA TRYLPGREGD YQRADESDLI
LEGYIAFLDP PKETTAPALK ALKASGITVK ILTGDSELVA AKVCHEVGLD AGEVVVGSSI
DALSDDELAT LAKRTTLFAR LTPMHKERIV TLLKREGHVV GFMGDGINDA PALRAADIGI
SVDGAVDIAR EAADIILLEK SLMVLEEGVI EGRRTFANML KYIKMTASSN FGNVFSVLVA
SAFLPFLPML PLHLLIQNLL YDVSQVAIPF DNVDDEQIQK PQRWNPTDLG RFMVFFGPIS
SIFDILTFCL MWWVFHANTP EVQTLFQSGW FIEGLLSQTL IVHMIRTRRI PFLQSRAAWP
LFAMTFVVMV VGIALPFSPL ASYLSLQALP LSYFPWLVLI LAGYMILTQT VKGFYSRRYG
WQ
//
