ID D8ML82_ERWBE Unreviewed; 894 AA.
AC D8ML82;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 78.
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=mgtB {ECO:0000313|EMBL:CAX61910.1};
GN OrderedLocusNames=EbC_43790 {ECO:0000313|EMBL:CAX61910.1};
OS Erwinia billingiae (strain Eb661).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=634500 {ECO:0000313|Proteomes:UP000008793};
RN [1] {ECO:0000313|EMBL:CAX61910.1, ECO:0000313|Proteomes:UP000008793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Eb661 {ECO:0000313|EMBL:CAX61910.1,
RC ECO:0000313|Proteomes:UP000008793};
RX PubMed=20565991; DOI=10.1186/1471-2164-11-393;
RA Kube M., Migdoll A.M., Gehring I., Heitmann K., Mayer Y., Kuhl H.,
RA Knaust F., Geider K., Reinhardt R.;
RT "Genome comparison of the epiphytic bacteria Erwinia billingiae and E.
RT tasmaniensis with the pear pathogen E. pyrifoliae.";
RL BMC Genomics 11:393-393(2010).
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 ---------------------------------------------------------------------------
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; FP236843; CAX61910.1; -; Genomic_DNA.
DR AlphaFoldDB; D8ML82; -.
DR STRING; 634500.EbC_43790; -.
DR KEGG; ebi:EbC_43790; -.
DR eggNOG; COG0474; Bacteria.
DR HOGENOM; CLU_002360_6_3_6; -.
DR Proteomes; UP000008793; 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 Hydrolase {ECO:0000313|EMBL:CAX61910.1};
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 Reference proteome {ECO:0000313|Proteomes:UP000008793};
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 75..93
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 105..122
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 281..299
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 311..335
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 763..786
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 828..848
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 864..882
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 18..91
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 894 AA; 98798 MW; 1D46673D703081A7 CRC64;
MKMNNANLNL ARDLAIASAA KQSLDSTLAR MHTQRQGLTQ EEAAERLAHY GKNQVANEKA
PHAIRQLFQA FNNPFIWVLM VLAGISFVTD YILPQRKGEE TDLTGVLIML MMVMLSGLLR
FWQEYRTNKA AEALKSMVRT TATVIRRSSA SAQPVRSEIA LHDVVPGDII FLSAGDMIPA
DVRLLSSRDL FVSQAALSGE AIPIEKYDAM ANIAEKTAAG SSDDADLLSM PGICLMGTNV
ASGTATAVVV ATGGETWFGS LAKSVVGSRP QTAFDRGVNS VSWLLIRFML VMVPIVLFIN
GFTKGDWSDA LMFALAVAVG LTPEMLPMIV SSNLAKGAIA MSRRKVVVKR LNAIQNFGAM
DVLCTDKTGT LTQDRIILEQ HLDAHGRNND KVLQLAWLNS RHQSGIKNLM DKAILSFSQG
NQAVAGLWRY RKIDELPFDF ERRRLSVVVA NEHNQQQLIC KGAVDEMLAV ASWWLDGGEK
RPLDEAARQQ WRQQAEEWNQ QGFRVLMLGE RELGDNPLTL PLSKADEREL TICGLLTFLD
PPKESAGEAI AALQESGVAV KVLTGDNAII TSKICREVGL NPGVPLCGTE IARLSDDELY
PLVEARTVFC RLTPQQKSRV LQALQYNGHT VGFLGDGIND APALRDADIG ISVDTATDIA
KESADIILLE KNLMVLEQGV IKGRETFGNI IKYLNMTASS NFGNVFSVLI ASAFIPFLPM
LAIHLLIQNL MYDLSQLALP WDKMDKEFLR KPRKWDAKNI GRFMLWMGPT SSLFDITTFV
IMWHVFAANS VEHQALFQSG WFIEGLLSQT LVVHMLRTQK IPFIQSRAAL PVMIATGLVM
ALGIYIPFSP LGHAVGLVPL PWSYFPWLVA TLFGYCVVAQ AMKRVYIRRF GQWF
//
