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Database: UniProt
Entry: L0G5S5_ECHVK
LinkDB: L0G5S5_ECHVK
Original site: L0G5S5_ECHVK 
ID   L0G5S5_ECHVK            Unreviewed;       833 AA.
AC   L0G5S5;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 65.
DE   SubName: Full=Heavy metal translocating P-type ATPase {ECO:0000313|EMBL:AGA80648.1};
GN   OrderedLocusNames=Echvi_4468 {ECO:0000313|EMBL:AGA80648.1};
OS   Echinicola vietnamensis (strain DSM 17526 / LMG 23754 / KMM 6221).
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC   Echinicola.
OX   NCBI_TaxID=926556 {ECO:0000313|EMBL:AGA80648.1, ECO:0000313|Proteomes:UP000010796};
RN   [1] {ECO:0000313|Proteomes:UP000010796}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17526 / LMG 23754 / KMM 6221
RC   {ECO:0000313|Proteomes:UP000010796};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Teshima H.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Echinicola vietnamensis DSM 17526.";
RL   Submitted (FEB-2012) 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}.
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DR   EMBL; CP003346; AGA80648.1; -; Genomic_DNA.
DR   RefSeq; WP_015268170.1; NC_019904.1.
DR   AlphaFoldDB; L0G5S5; -.
DR   STRING; 926556.Echvi_4468; -.
DR   KEGG; evi:Echvi_4468; -.
DR   PATRIC; fig|926556.3.peg.4719; -.
DR   eggNOG; COG2217; Bacteria.
DR   HOGENOM; CLU_001771_6_0_10; -.
DR   OMA; HLHLMET; -.
DR   OrthoDB; 1488806at2; -.
DR   Proteomes; UP000010796; Chromosome.
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   CDD; cd07551; P-type_ATPase_HM_ZosA_PfeT-like; 1.
DR   Gene3D; 3.30.70.100; -; 2.
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; 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; 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; TIGR01525; ATPase-IB_hvy; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 1.
DR   PANTHER; PTHR48085; CADMIUM/ZINC-TRANSPORTING ATPASE HMA2-RELATED; 1.
DR   PANTHER; PTHR48085:SF5; CADMIUM/ZINC-TRANSPORTING ATPASE HMA4-RELATED; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00120; HATPASE.
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   PROSITE; PS00154; ATPASE_E1_E2; 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:UP000010796};
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        198..217
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        223..241
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        441..460
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        472..496
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        786..805
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        811..830
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   REGION          161..189
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          357..381
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   833 AA;  89985 MW;  607F9BB9F64E3955 CRC64;
     MKKLQIKIPL LLPEVPDEKD QCVAKLIERL KNKEGLEKVH IADETDNGVP QLCFHYDPEL
     ISIDRIQSLA EQTGAEITRK FGHKLIEVDG IRHTRHARNI ERGLRGIAGI MEASVSASGM
     VRVEYDTAKT DEAEILKALR KDGLDMPDTQ VSAERFLEQV KETEKGEDQK EGNKEHVHEE
     GEDHDHSHGG IFGKNTELIF SIICGALLGI GFGLTYIEAV PSWVSLSLYI GAYFFGGYFT
     AKEAIQTVAK GGFEIDFLML VAAIGAAILG EWAEGALLLF LFSMGHALEH YAMNKARKSI
     AALAELAPKT ALLKRNGKTE EVGIEELSIG DIIVVKPNSK ISADGVVISG QSSVNQAPIT
     GESVPVDKEP VDNPDKDWSQ EDDIKDENRA FSGTINGNNT LEIKVIKVAK DSTLSRLVKL
     VNEAQTQKSP TQRLTDKFEK YFVPSVLVLV VLLNFAFLVI DESFSESFYR AMAVLVAASP
     CALAIATPSA VLSGVARAAK SGVLIKGGRP LEDLGVLTAL AFDKTGTLTE GKPKLTEVVA
     VGDVKEDELL KIAVAVESLS DHPLAKAVVR DGKERLDGAD VPDAKDLEAV LGKGIKATLG
     DDKVYIGNLD LFESLDDNKP EKETEEKVKS LESDGNTTML IRQNDHYIGI IALMDTPRKE
     AKNTLEQLKK IGIKRMIMLT GDNQKVADAV AKEIGLTDAW GSLLPEEKVE AIKKLKKNES
     KVAMVGDGVN DAPAMANSTV GIAMGAAGSD VALETADIAL MADKLETLPF AIALSRNAKS
     IIKQNLWISL GIVGILIPLT ISGIATIGPA VLIHEGSTLV VVFNALRLLA YKK
//
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