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
//