ID M7P242_9GAMM Unreviewed; 811 AA.
AC M7P242;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE SubName: Full=Heavy metal translocating P-type ATPase {ECO:0000313|EMBL:EMR13547.1};
GN ORFNames=MPL1_04487 {ECO:0000313|EMBL:EMR13547.1};
OS Methylophaga lonarensis MPL.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Methylophaga.
OX NCBI_TaxID=1286106 {ECO:0000313|EMBL:EMR13547.1, ECO:0000313|Proteomes:UP000012019};
RN [1] {ECO:0000313|EMBL:EMR13547.1, ECO:0000313|Proteomes:UP000012019}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MPL {ECO:0000313|EMBL:EMR13547.1,
RC ECO:0000313|Proteomes:UP000012019};
RX PubMed=23661481;
RA Shetty S.A., Marathe N.P., Munot H., Antony C.P., Dhotre D.P.,
RA Murrell J.C., Shouche Y.S.;
RT "Draft Genome Sequence of Methylophaga lonarensis MPLT, a Haloalkaliphilic
RT (Non-Methane-Utilizing) Methylotroph.";
RL Genome Announc. 1:E00202-13(2013).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU362081}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IB subfamily. {ECO:0000256|ARBA:ARBA00006024,
CC ECO:0000256|RuleBase:RU362081}.
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:EMR13547.1}.
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DR EMBL; APHR01000020; EMR13547.1; -; Genomic_DNA.
DR RefSeq; WP_009725915.1; NZ_APHR01000020.1.
DR AlphaFoldDB; M7P242; -.
DR STRING; 1286106.MPL1_04487; -.
DR PATRIC; fig|1286106.3.peg.900; -.
DR eggNOG; COG2217; Bacteria.
DR OrthoDB; 9814270at2; -.
DR Proteomes; UP000012019; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015662; F:P-type ion transporter activity; IEA:UniProt.
DR CDD; cd00371; HMA; 1.
DR Gene3D; 3.30.70.100; -; 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; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR021993; ATPase-cat-bd.
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; IPR017969; Heavy-metal-associated_CS.
DR InterPro; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_sf.
DR InterPro; IPR027256; P-typ_ATPase_IB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01511; ATPase-IB1_Cu; 1.
DR NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR43520; ATP7, ISOFORM B; 1.
DR PANTHER; PTHR43520:SF5; CATION-TRANSPORTING P-TYPE ATPASE-RELATED; 1.
DR Pfam; PF12156; ATPase-cat_bd; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00403; HMA; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00943; CUATPASE.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 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; SSF55008; HMA, heavy metal-associated domain; 1.
DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 1.
DR PROSITE; PS50846; HMA_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362081};
KW Cell membrane {ECO:0000256|RuleBase:RU362081};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362081};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU362081};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW Reference proteome {ECO:0000313|Proteomes:UP000012019};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362081};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362081}.
FT TRANSMEM 173..194
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 206..227
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 239..257
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 269..287
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 422..442
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 448..468
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 759..779
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 785..803
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 89..155
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 811 AA; 87296 MW; 588ADCDEF257D697 CRC64;
MSESCYHCGL PVTTPGTFHA VLAGESRNFC CHGCKTVCQS IHDAGLESFY QKTPEGELLA
PPPDIPQELA AYDLDEVQSD YVDGMQQHRT INLLVEGIHC AACVWLIEHA LAKQPGVDAA
DVNLTAKRLR LRWDNNKTSL SAVLGKLAQI GYAAVPFDPE TAEGALAKRH RSLVYRMAFA
GFAMMNILWV SIALYTGAAQ DEFRHWFHWV GFAIATPTLL YSGYPFFRNA IVGLRSAYLT
MDLPIAIGAT VTYLYSVYIT VSGSTAGEVY FDTVVNFLFV ILVGRYLEAI SKRNALSATR
RMLELQPKLA TVVREDGTTA ILPIRSVVPG DLLLVRPGEK IPVDGYIEEG ESAVDESMLS
GESVPVAKSI NDKVVAGTLN GEGAFKVRAE FVVRGTMLAK IVAMMDDAQA SKSPLQSTAD
RIVPWFVLVT LTLATLTFVY WVQYDFAIAL LAAASVMVIT CPCAFGMATP MSIAVATGVG
ATRGILVKHG AVLERLSDAT HFVFDKTGTL TEGKLRVVKI ESLSEMSEAR LLELAASAEQ
NSEHSIATAI VCLAEQRGVS LMEATSFSAT PGRGVSCLVA DQSVIVGTRE WLAMQNIEVS
ETVTEKQSAF EKAGVTCVFV AVDGKVAGLI GVEDTLRHDA QQLIDALKAQ GIAITVLSGD
RQAVVDAVTA RFGNIERRAQ VLPQDKSAVI RQLQEQGEVV AMVGDGINDS PALIQSDIGI
ALASGTDVSI ESADIVLSHN ELIQVDASRR LAKRTLKTIR QNIVLSFTYN VIMVPLAMMA
LVSPLVAAIT MPISSLVVIG NAARISRMFK G
//
