Unfortunately due to lack of commercial feasibility, the SkyBLAST service has been suspended from December 1st, 2025.
All subscriptions for paid accounts have been paused. For further information or enquiries, please email [email protected]
LOCUS WP_010989665 707 aa linear BCT 24-MAR-2023 ACCESSION WP_010989665 VERSION WP_010989665.1 KEYWORDS RefSeq. SOURCE Listeria monocytogenes ORGANISM Listeria monocytogenes Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria. REFERENCE 1 (residues 1 to 707) AUTHORS Bublitz,M., Morth,J.P. and Nissen,P. TITLE P-type ATPases at a glance JOURNAL J Cell Sci 124 (Pt 15), 2515-2519 (2011) PUBMED 21768325 REMARK Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917] REFERENCE 2 (residues 1 to 707) AUTHORS Palmgren,M.G. and Nissen,P. TITLE P-type ATPases JOURNAL Annu Rev Biophys 40, 243-266 (2011) PUBMED 21351879 REFERENCE 3 (residues 1 to 707) AUTHORS Apell,H.J. TITLE How do P-type ATPases transport ions? JOURNAL Bioelectrochemistry 63 (1-2), 149-156 (2004) PUBMED 15110265 COMMENT REFSEQ: This record represents a single, non-redundant, protein sequence which may be annotated on many different RefSeq genomes from the same, or different, species. ##Evidence-For-Name-Assignment-START## Evidence Category :: Conserved Domain (CDD) Evidence Accession :: Domain architecture ID 11534186 Evidence Source :: NCBI SPARCLE ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..707 /organism="Listeria monocytogenes" /db_xref="taxon:1639" Protein 1..707 /product="heavy metal translocating P-type ATPase" /EC_number="7.2.2.-" /GO_function="GO:0005524 - ATP binding [Evidence IEA]" /GO_function="GO:0015662 - P-type ion transporter activity [Evidence IEA]" /GO_function="GO:0016887 - ATP hydrolysis activity [Evidence IEA]" /GO_function="GO:0019829 - ATPase-coupled monoatomic cation transmembrane transporter activity [Evidence IEA]" /GO_function="GO:0046872 - metal ion binding [Evidence IEA]" /calculated_mol_wt=76347 Region 9..69 /region_name="HMA" /note="Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid residues found in a number of proteins that transport or detoxify heavy metals, for example, the CPx-type heavy metal ATPases and copper chaperones. HMA domain...; cd00371" /db_xref="CDD:238219" Site order(15..17,20) /site_type="metal-binding" /note="metal-binding site [ion binding]" /db_xref="CDD:238219" Region 109..704 /region_name="P-type_ATPase_Cd-like" /note="P-type heavy metal-transporting ATPase, similar to Staphylococcus aureus plasmid pI258 CadA, a cadmium-efflux ATPase; cd07545" /db_xref="CDD:319845" Site order(354,356,666..667,688,692) /site_type="other" /note="putative HM ion binding site [ion binding]" /db_xref="CDD:319845" Site order(398..400,466,482..484,513,554..556,576,579,582,601, 604) /site_type="other" /note="putative ATP binding site [chemical binding]" /db_xref="CDD:319845" ORIGIN 1 mskaskqtty rvdgmsctnc agkfeknvkn legvtdakvn fgagkisvyg etsisqieka 61 gafenlrvtd ekdysskpak kesflkknwh lvvsiifiil afisqnisge dstttiilyv 121 iaivvggfnl fkegfanlik ldftmeslmt iaiigasiig ewaegsivvi lfafsevler 181 ysmdkarqsi rslmdiapke alirrddveq miavsdiqig dimiikpgqk iamdgvvikg 241 ysainqsait gesipvekkv ddevfagtln eegllevkvt khvedttisk iihlveeaqg 301 erapaqafvd kfakyytpti mliallvvvv pplffggdwd twvyqglsll vvgcpcslvi 361 stpvsivsai gnsakngvlv kggiyleeig glqaiafdkt gtltkgkpvv tdfipysehm 421 deqnslsiit aletmsqhpl asaiiskami dnvdyksiei dnfssitgkg vkgevngity 481 yigssklfes sleksqsisq tyqslqkqgk tamlfgtesn ilaiiavade vresskevia 541 qlhklgiaht imltgdnndt aqfigkeigv sdikaelmpe dkltyikelk qtygkvamig 601 dgvndapala astvgiamgg agtdtaleta dvalmgddlk klpfivnlsr ktlkiikqni 661 tfslgiklla lllvlpgwlt lwiaivadmg atllvtlngl rlmkvkk