ID A0A095ZN55_9BACT Unreviewed; 616 AA.
AC A0A095ZN55;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Metal ABC transporter ATPase {ECO:0000313|EMBL:KGF36205.1};
GN ORFNames=HMPREF2137_02745 {ECO:0000313|EMBL:KGF36205.1};
OS Hoylesella buccalis DNF00853.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Hoylesella.
OX NCBI_TaxID=1401074 {ECO:0000313|EMBL:KGF36205.1, ECO:0000313|Proteomes:UP000029556};
RN [1] {ECO:0000313|EMBL:KGF36205.1, ECO:0000313|Proteomes:UP000029556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DNF00853 {ECO:0000313|EMBL:KGF36205.1,
RC ECO:0000313|Proteomes:UP000029556};
RA McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (JUL-2014) 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:KGF36205.1}.
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DR EMBL; JRNN01000029; KGF36205.1; -; Genomic_DNA.
DR RefSeq; WP_036871936.1; NZ_JRNN01000029.1.
DR AlphaFoldDB; A0A095ZN55; -.
DR OrthoDB; 1521937at2; -.
DR Proteomes; UP000029556; 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 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 NCBIfam; TIGR01512; ATPase-IB2_Cd; 1.
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 HMA2; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
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 Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362081};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362081}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 39..58
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 243..262
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 568..587
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
SQ SEQUENCE 616 AA; 67248 MW; 3E9B79B979CA3F28 CRC64;
MEDIHEEEQM AWWKIILSGV MLVVGIAAPY IGLTILDNQW ISLAWYVVAF AFVGLPVMKE
AWECAVKGDV FSEFMLMTIA CIGAFAIGEY PEAVAVMLLY CIGEALQDRA VDRARDNIRA
LVAFRPTIAR VVVDGTTVEK QPAEVAVGDV IEVKAGERVP LDGTLLSESA SLNTAALTGE
SMPRTMEKGE EVMAGMIAVD QVLRLKVTRP ESQSAISRIL KMVEDAAERK APTELFIRRF
ARIYTPIVVM LAALAILLPY LYSLFDANFT YVFSEWFRRA LVFLVISCPC ALVISVPLGY
FAGIGSASKR GILFKGSNYL DAITEVDLVM FDKTGTLTTG EFAVQSVEGL DEEALKTVSA
IEKSSNHPIA KAIVRYCPTD EKIDAKDIAG HGLQTDEWLV GNLKLLEREN VFFPDALRNI
PETVVCVAHL GRYVGHIILA DKVKDDAKQA VESLPVRVEM LSGDRQELVS KVASSLGIRK
AYGDLLPEGK VKHIEQAKHM GQRVAFVGDG INDAPVLALS DVGIAMGGLG SDMAIETADI
IIQTDQPSKV ADAIRIGKYT RRIVNQNIWL ALIIKALVML LGLLGLANLW MAVFADSGVA
LLAVLNSSRI FLKNNK
//
