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Database: UniProt
Entry: A0A013VPV8_9SPHN
LinkDB: A0A013VPV8_9SPHN
Original site: A0A013VPV8_9SPHN 
ID   A0A013VPV8_9SPHN        Unreviewed;       754 AA.
AC   A0A013VPV8;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   SubName: Full=Haloacid dehalogenase {ECO:0000313|EMBL:EXS70512.1};
GN   ORFNames=BF95_18480 {ECO:0000313|EMBL:EXS70512.1};
OS   Sphingobium sp. Ant17.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=1461752 {ECO:0000313|EMBL:EXS70512.1, ECO:0000313|Proteomes:UP000021537};
RN   [1] {ECO:0000313|EMBL:EXS70512.1, ECO:0000313|Proteomes:UP000021537}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ant17 {ECO:0000313|EMBL:EXS70512.1,
RC   ECO:0000313|Proteomes:UP000021537};
RA   Adriaenssens E.M., Cowan D.A.;
RT   "Draft genome sequence of the aromatic hydrocarbon-degrading bacterium
RT   Sphingobium sp. strain Ant17 isolated from Antarctic soil.";
RL   Submitted (FEB-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:EXS70512.1}.
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DR   EMBL; JEMV01000016; EXS70512.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A013VPV8; -.
DR   STRING; 1461752.BF95_18480; -.
DR   PATRIC; fig|1461752.3.peg.2105; -.
DR   Proteomes; UP000021537; 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   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0015662; F:P-type ion transporter activity; IEA:UniProt.
DR   CDD; cd02094; P-type_ATPase_Cu-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   Gene3D; 1.10.620.20; Ribonucleotide Reductase, subunit A; 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; IPR009078; Ferritin-like_SF.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR045800; HMBD.
DR   InterPro; IPR027256; P-typ_ATPase_IB.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   InterPro; IPR012348; RNR-like.
DR   InterPro; IPR007029; YHS_dom.
DR   NCBIfam; TIGR01511; ATPase-IB1_Cu; 1.
DR   NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 1.
DR   PANTHER; PTHR43520; ATP7, ISOFORM B; 1.
DR   PANTHER; PTHR43520:SF8; COPPER-TRANSPORTING ATPASE 2; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF19335; HMBD; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   Pfam; PF04945; YHS; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00943; CUATPASE.
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; SSF47240; Ferritin-like; 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   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        99..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        132..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        163..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        202..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        356..378
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        384..407
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        700..719
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        725..747
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          1..40
FT                   /note="YHS"
FT                   /evidence="ECO:0000259|Pfam:PF04945"
FT   DOMAIN          54..80
FT                   /note="Heavy metal binding"
FT                   /evidence="ECO:0000259|Pfam:PF19335"
SQ   SEQUENCE   754 AA;  79622 MW;  0F2BE39AF913582C CRC64;
     MTVDPEKTTH HVEHGGATYY FCSSDCRAKF VTDPGRYVGS TSVPQHETEA GTIWTCPMHP
     EVRQDHPGNC PICGMTLEPA IVTADAGPSP ELADMSRRFW IGLILALPVL ILEMGGHIFP
     ALHHLVPMRI SAWIQLVLAT PVVLWAGWPF FERAWTSVRT RNLNMFTLIA MGTGIAWAYS
     IVATLAPGVF PPAFRSADGT VAIYFEAAAV ITVLVLLGQV LELRARERTS GAIKALLNLA
     PKTARRISAA GADEEVGLDQ IVVGDRLRVR PGEKVPVDGI VEDGRSSLDE SMVTGESMPI
     TKTVADKVIG GTLNQTGALV IRADKVGRDT MLARIVQMVA EAQRSRAPIQ RMADRVSGWF
     VPVVLAIAVL AFAGWAIWGP EPRFAYGLVA AVAVLIIACP CALGLATPMS IMVGVGRGAG
     LGVLIKNAEA LERMEKVDTL VVDKTGTLTE GHPSVTKIVA GAGFSEDEVL RLAAGVERAS
     EHPLARAIVE AANARQIPIP EVADFDSPTG KGALGTVEGK RVLLGNTAFL KEHGVETALL
     DAEADELRRD GATAIFAGID GVVAGVLAIA DPIKKTTPEA LAGLRAEGIR VVMLTGDNRT
     TAEAVARTLG IDEVEAEVLP DQKSAVVERL KREGRIVAMA GDGVNDAPAL AAAEVGIAMG
     SGTDVAIESA GITLLKGDLM GIVRARRLSQ ATMSNIRQNL VFAFIYNAAG IPVAAGLLYP
     VFGILLSPMI AAAAMALSSV SVVTNALRLN RRKI
//
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