ID K5YAX6_9BACT Unreviewed; 646 AA.
AC K5YAX6;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Heavy metal translocating P-type ATPase {ECO:0000313|EMBL:EKN10502.1};
GN ORFNames=HMPREF1077_01753 {ECO:0000313|EMBL:EKN10502.1};
OS Parabacteroides johnsonii CL02T12C29.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC Parabacteroides.
OX NCBI_TaxID=999419 {ECO:0000313|EMBL:EKN10502.1, ECO:0000313|Proteomes:UP000001218};
RN [1] {ECO:0000313|EMBL:EKN10502.1, ECO:0000313|Proteomes:UP000001218}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL02T12C29 {ECO:0000313|EMBL:EKN10502.1,
RC ECO:0000313|Proteomes:UP000001218};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Zitomersky N.L., Coyne M.J.,
RA Comstock L.E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D.,
RA Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Parabacteroides johnsonii CL02T12C29.";
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}.
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:EKN10502.1}.
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DR EMBL; AGZP01000016; EKN10502.1; -; Genomic_DNA.
DR RefSeq; WP_008156284.1; NZ_JH976466.1.
DR AlphaFoldDB; K5YAX6; -.
DR PATRIC; fig|999419.3.peg.1794; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_6_2_10; -.
DR OrthoDB; 1521937at2; -.
DR Proteomes; UP000001218; 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 InterPro; IPR044492; P_typ_ATPase_HD_dom.
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 PRINTS; PR00943; CUATPASE.
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:UP000001218};
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 26..44
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 56..75
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 87..113
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 256..277
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 289..314
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 598..617
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 623..641
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
SQ SEQUENCE 646 AA; 69943 MW; 939E8A2F245BD1AF CRC64;
MEAKTTCHSG YGCGHGHNKG EKRWEIALPI LSFILLIAGL ILDHTGQSWF SPAAKLVWYL
TAFLPVGLPV MREAYREALQ KDFFTEFSLM SIASIGAFSI GEYPEAVAVM LFYTVGEMLQ
NKAVERASQN ISRLLDVRPE RTDVFREGKY INVSPKEVKT GERIEVKPGG RIPLDGILQE
TEASFDTSAL TGESMPRTLR KGDEVLAGMI VLGQAVRIEV NRPYDQSALA RILALVKDAA
ERKAPAELFI RRFARFYTPA VIVLALLIVI VPALAGLVVP SFQYVFHDWL YRGLVFLVIS
CPCALVISVP LGYFGGIGAA SQAGILFKGG NYLDAITRIN TVAFDKTGTL TTGRFEVTDM
LAHGISEPEL LALLLSVEQK STHPIAQAIV RYAKKQNISA INISEMHELA GHGMEAIIGG
QEVLVGNIRL MTERGISIPE ELSDKVATVV ICAIGKKYTG HLLLSDTLKD DAVEAIAKLR
KLGVTDIRLL SGDKKEIVES FAKRLDIDLA YGNLLPEDKA THIREMVEEP GKSVAFVGDG
MNDAPVLALS HVGIAMGGLG SDAAIESADV VIQNDQPSKV ATAIAIGRKT RTIVRQNIIG
ALGVKGIVLL AGALGYVTLW GAVFADVGVA LLAVFNSVRI LNRKVW
//
