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Entry: W7CZH8_9LIST
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ID   W7CZH8_9LIST            Unreviewed;       884 AA.
AC   W7CZH8;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 45.
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=BCAMP_04125 {ECO:0000313|EMBL:EUJ41171.1};
OS   Brochothrix campestris FSL F6-1037.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Brochothrix.
OX   NCBI_TaxID=1265861 {ECO:0000313|EMBL:EUJ41171.1, ECO:0000313|Proteomes:UP000019243};
RN   [1] {ECO:0000313|EMBL:EUJ41171.1, ECO:0000313|Proteomes:UP000019243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL F6-1037 {ECO:0000313|EMBL:EUJ41171.1,
RC   ECO:0000313|Proteomes:UP000019243};
RA   den Bakker H.C., Allred A., Warchocki S., Wright E.M., Burrell A.,
RA   Nightingale K.K., Kephart D., Wiedmann M.;
RT   "Novel taxa of Listeriaceae from agricultural environments in the United
RT   States.";
RL   Submitted (DEC-2012) 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}.
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:EUJ41171.1}.
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DR   EMBL; AODH01000013; EUJ41171.1; -; Genomic_DNA.
DR   AlphaFoldDB; W7CZH8; -.
DR   STRING; 1265861.BCAMP_04125; -.
DR   PATRIC; fig|1265861.3.peg.811; -.
DR   OrthoDB; 9760364at2; -.
DR   Proteomes; UP000019243; 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; 2.
DR   PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR42861:SF29; SECRETORY PATHWAY CALCIUM ATPASE, ISOFORM G; 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   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019243};
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}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        67..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        98..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        261..279
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        291..315
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        678..694
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        740..763
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        783..806
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        818..840
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        852..871
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          14..88
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
SQ   SEQUENCE   884 AA;  97077 MW;  A29D3132B19FC6C6 CRC64;
     MTKKTITPSQ NKYDFATRAS EEELFSYFNS AHTGLTTEAV TQSLTEYGEN RLEAVNQTPY
     WRIVMKAFLN PFTIVLIALA FISFITDYTL ATAADKDMTA VIIIMTMVIL SGSVSLFQTV
     KTNKSLEQLQ NMIEVTAAVR RNGHKAVEQP IESLVVGDII ELSAGDMLPA DLRIIEAKDL
     FVSQASMTGE SVPVEKNGAR AMPTKSKLEA ENLVFMGSNV VSGTAVGIII AVGQATQFGQ
     IATDISAVKL KTSFEKGVGS VSWLLIRFML LMAPTVFIIN GLTKGDWLEA LMFGLSVAVG
     LTPEMLPMIV TANLVKGTAA MAKQGTIIKN INAIQNFGAM DVLCTDKTGT ITQDKVTLQY
     HLNVNGKEDD RILRHGFYNS FYQTGLKNLM DVAIIAEAEK QLAVNTDNYQ KIDEIPFDFN
     RRRMSVVIKN QKGETEVITK GAVEEMLAIS TTVEFDGHIL PLDEDMRAKL LRAVTQLNEQ
     GLRVIAIAQK KTNPQDHAFC IADEAEMTLM GYLAFLDPPK ETAQAAISSL QSFGVAVKVL
     TGDNAEVTRT VCRQVGLTTE NFFHGHDLDE LSDIELENIV LDYQVFVKLS PSQKTRIVQA
     LQANGKVVGF MGDGINDAAA MRTADIGISV DTAVDIAKES ADVILLEKDL NVLEKGMLEG
     RHLFGNIVKY IKMTASSNFG NMFSVLVASI FLPFLPMLPI QILCLNLIYD TTCISLPWDK
     VDRSYLAKPR KWEAKSIGNF MRWIGPTSSI FDIITFVLLF FIICPQVVGG QFSTLTGSEQ
     VVFIALFHAG WFVESLWSQT LVIHALRTEK IPFLQSNAAR IVTCVTAIGI LMGTVLPYTA
     VGTTLGMSAL PLSYFAWLAA IILAYLALVS VMKGVYIRRF GELL
//
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