ID A0A0X8GYD7_9FIRM Unreviewed; 667 AA.
AC A0A0X8GYD7;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Metal-transporting ATPase {ECO:0000313|EMBL:AMC92694.1};
GN ORFNames=AOC36_01430 {ECO:0000313|EMBL:AMC92694.1};
OS Erysipelothrix larvae.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Erysipelothrix.
OX NCBI_TaxID=1514105 {ECO:0000313|EMBL:AMC92694.1, ECO:0000313|Proteomes:UP000063781};
RN [1] {ECO:0000313|EMBL:AMC92694.1, ECO:0000313|Proteomes:UP000063781}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LV19 {ECO:0000313|EMBL:AMC92694.1,
RC ECO:0000313|Proteomes:UP000063781};
RA Lim S., Kim B.-C.;
RT "Erysipelothrix larvae sp. LV19 isolated from the larval gut of the
RT rhinoceros beetle, Trypoxylus dichotomus.";
RL Submitted (OCT-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}.
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DR EMBL; CP013213; AMC92694.1; -; Genomic_DNA.
DR RefSeq; WP_067630386.1; NZ_CP013213.1.
DR AlphaFoldDB; A0A0X8GYD7; -.
DR STRING; 1514105.AOC36_01430; -.
DR KEGG; erl:AOC36_01430; -.
DR OrthoDB; 9813266at2; -.
DR Proteomes; UP000063781; 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; 3.40.1110.10; 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; 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; PTHR43079:SF1; CADMIUM_ZINC-TRANSPORTING ATPASE HMA1, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR43079; PROBABLE CADMIUM/ZINC-TRANSPORTING ATPASE HMA1; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
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 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:UP000063781};
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 51..71
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 77..95
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 107..125
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 131..148
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 282..304
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 310..334
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 614..635
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 641..662
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 667 AA; 72545 MW; FE61ED5FFFB131BC CRC64;
MTHQAHTHET CHHDHAHHDH HGHDHHGHDH HHEHDHAHGH HHDHNHNSPG LIAAYFVGLA
LYIVALLIPQ GFLRNTLYVA TLLFSGLHII LEGFQDTYYA TKSNHKFTPN VHVLMTLAAF
GAIIIGEYQE AALLILIFAG AHFLEGYAEG RSKKEITNLL KLKPTQARLL NQDGSITLVD
VSTLKIGDHL QVLSGDQIAT DGFIISGWAT IDQSSITGES IPVDKQTGDL VFGSTINGNT
VFEMEVSKDS SDTVFAKIVA LVSQAQSNIS KTAVLIKRIE PIYVTGVLIA APIFYLLGLS
VFGWGHTMSF YRTMVMLIVA SPCALAATDI PATLSAISNL AKRGVLFKGG SYLSNLSDIK
VVAFDKTGTL TEGKPVVTDV QFTDALDPKQ QKQALNIFVN MERKSNHPLA DAITAHFKDE
PILDIEVINL IGSGLSARYD SRSYIIGKPS VFSDINADIQ SKTRQLEDDG KTVIYLSIDS
SVVGLIAIQD IPKQSAAHAI QYFKDNNVHT VMLTGDAKQT GEAIGKQLGI DEIIANVLPE
DKATIITSLQ SKHGPIAMLG DGVNDAPALV NADIGVAMGD GTDIAIDAAD AVLMENDLSK
FVYTHKLSKK LRRVVIQNII FAMGVVVFLL IMNIIGQMDM WFAVLMHEGS TILVILSGLR
LLKGIQE
//
