ID A0A1A9T332_9PROT Unreviewed; 803 AA.
AC A0A1A9T332;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=ATPase P {ECO:0000313|EMBL:OAM52415.1};
GN ORFNames=A7981_02735 {ECO:0000313|EMBL:OAM52415.1};
OS Methylovorus sp. MM2.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Methylophilaceae; Methylovorus.
OX NCBI_TaxID=1848038 {ECO:0000313|EMBL:OAM52415.1, ECO:0000313|Proteomes:UP000077545};
RN [1] {ECO:0000313|Proteomes:UP000077545}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MM1 {ECO:0000313|Proteomes:UP000077545};
RA Macey M.C., Murrell J.C.;
RT "Draft genome of Methylovorus sp. MM1 isolated from grassland soil.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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:OAM52415.1}.
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; LXUF01000001; OAM52415.1; -; Genomic_DNA.
DR RefSeq; WP_067263682.1; NZ_LXUF01000001.1.
DR AlphaFoldDB; A0A1A9T332; -.
DR STRING; 1848038.A7981_02735; -.
DR OrthoDB; 8552577at2; -.
DR Proteomes; UP000077545; 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 CDD; cd02079; P-type_ATPase_HM; 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; 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; TIGR01512; ATPase-IB2_Cd; 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; SFLDG00002; C1.7:_P-type_atpase_like; 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 PROSITE; PS00154; ATPASE_E1_E2; 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|RuleBase:RU362081};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW Reference proteome {ECO:0000313|Proteomes:UP000077545};
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 182..202
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 214..235
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 273..292
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 426..448
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 454..477
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 759..776
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 782..800
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 94..160
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 803 AA; 86533 MW; 626D1A267D17D229 CRC64;
MNADIACYHC GLPLTPGASF STTVFNIPRA MCCHGCQAVA ESIVANGLQD YYTYRTELPK
TADELVPEEL RQLDLYDHPE VQKSFVLETN HDIKEASLIL EGITCAACIW LNERHLKQLK
GVRNVAFNYA SQRARISWDD RDIKLSRILA EIRKLGYHAH PFSAQQQDLL RQAQRKSDFR
RLAVAGLSAG QVMMIAVALY AGADQGLEYA TGQLLRGLSL VLSLPAMTYA AWPFYKAAWR
GIVNHKIGMD VPIVLGLVTG FIGSIWATLH GGVVYYDTLT MLIFFLLTTR YLERNAREKS
IEAAENLLRL APAMATRVDG EQQTLIPLVE LHEGDLILAR PGETIAADGI VMEGESSADE
SLLTGESKPL RKIAGSHVYT GSINYESPLL IRVTGVGENT MLAGISRLLD RAQAEKPKLA
QTADLVAAYF TYALLVVVAI VATTWWLIEP QRVLEIVLTV LVVSCPCALS LAAPAAFAAA
GSHLIERGVL LTRGHALETL SKVTHFVFDK TGTLTVGRPV LLQVIPLVDL AVDECLKIAA
SLEQSSEHPI AKSFIDAMQH QPLHIVAESL NTPSQGVSGV INGKTYRIGN AALHGDIGKH
ADVRLADGQP GASIVWLSDA ETLLAAFVLA DSPRPDAAEL IVALKAKGFE VSILSGDAPA
AVAHFAKSLN IAHWQAALSP AQKLSTLQEL QSRGAVVAMV GDGINDAPVL AGAQVSIAMG
SGTQMARASG DIVLLTEKLV EIEHAVTTSV FGISVIRQNF IWALAYNLIA LPFAALGWLS
PWMAAIGMSV SSLIVVLNAL RLR
//
