ID A0A0X3TA41_9GAMM Unreviewed; 844 AA.
AC A0A0X3TA41;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=ATPase P {ECO:0000313|EMBL:KUJ72642.1};
GN ORFNames=AVO41_02230 {ECO:0000313|EMBL:KUJ72642.1};
OS Thiomicrospira sp. WB1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Thiomicrospira.
OX NCBI_TaxID=1685380 {ECO:0000313|EMBL:KUJ72642.1, ECO:0000313|Proteomes:UP000053531};
RN [1] {ECO:0000313|EMBL:KUJ72642.1, ECO:0000313|Proteomes:UP000053531}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WB1 {ECO:0000313|EMBL:KUJ72642.1,
RC ECO:0000313|Proteomes:UP000053531};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-2015) 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:KUJ72642.1}.
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; LQBN01000001; KUJ72642.1; -; Genomic_DNA.
DR RefSeq; WP_068581930.1; NZ_LQBN01000001.1.
DR AlphaFoldDB; A0A0X3TA41; -.
DR STRING; 1685380.AVO41_02230; -.
DR OrthoDB; 9814270at2; -.
DR Proteomes; UP000053531; 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; 2.
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; 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:UP000053531};
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 174..199
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 211..229
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 241..259
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 271..289
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 425..446
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 452..472
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 774..791
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 797..815
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 90..156
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 844 AA; 92945 MW; 8C57730D7F7DA3FB CRC64;
MSETSCFHCG QPALKASQVI QPIQGESQVF CCHGCAGVCE AIHEAGMEGF YRRTPEGELL
SPPPPPTPNA DFYDYDEVQS QFVTSLDSRR SITLMSEAIH CAACIWLIEH TLAKLDGVLM
AKVNFTNKQI KIRWDNERIQ LSDIIHALNR IGYDATPYDA SASEEAYRKA NRDLLYRLGF
AGFAMMNVMW FAVALYAGAD EDPEFRHYFH WVQWVIATVT LIYSGKPFWR GAWQSLKARN
VGMDVSITLG ILTTYFYSFW VTIDPTHSGD VYFDTMIDFI FLLLIGRYLE AISKNKAMDS
TRRLMDLQPK VARQIEGQND QVSVVPVRKL KPGDRVMVKP GDQIPVDGVV LTGTGNVNES
MLSGESREIA KQPGMRVSAG TLNLDGTLTI EVSAILQGTM LGRIVSMVED AQGAKAPIQC
TAEKIMPWFV SVVITLAVLS FAYWIVHADL ETAMIAATAV LIITCPCAFG LATPMATAVA
SGVSAQNGIL IKNASVLEVL QQMNHFVFDK TGTLTQGKMQ LQELIWADQA PADEAGRSHL
IEAMVRIEFH SEHSLGKAIV EALQAQYPAL KNERMTLDRF QAHPGRGVEA DWQGRHYLIG
TRAWLSQYQV DFPPGLVKKE AERGAVGETS VWVVRDGQVQ AVLFLKDPLR EDARALIDRL
KVKGKQVTLL SGDRQAVAES VAKELGGMEV IAEVLPDEKH DVIARLQQTQ PVVMVGDGVN
DAPALARARV SMALGSGTDV SMDCADVILL NNELLSVDTA LALSQRTLKT IKENIISSII
YNVTFVPLAM AALLTPLIAA ITMPLSSLVV ILNAARIRRF FHPKAIRQRE AEAQEAMIKA
PEPD
//
