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Database: UniProt
Entry: K4L6N9_9FIRM
LinkDB: K4L6N9_9FIRM
Original site: K4L6N9_9FIRM 
ID   K4L6N9_9FIRM            Unreviewed;       848 AA.
AC   K4L6N9;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Cadmium-transporting ATPase {ECO:0000313|EMBL:AFV06266.1};
DE            EC=3.6.3.3 {ECO:0000313|EMBL:AFV06266.1};
GN   ORFNames=DCF50_p2263 {ECO:0000313|EMBL:AFV06266.1};
OS   Dehalobacter sp. CF.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Dehalobacter.
OX   NCBI_TaxID=1131462 {ECO:0000313|EMBL:AFV06266.1, ECO:0000313|Proteomes:UP000000482};
RN   [1] {ECO:0000313|EMBL:AFV06266.1, ECO:0000313|Proteomes:UP000000482}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF {ECO:0000313|EMBL:AFV06266.1};
RX   PubMed=23284863; DOI=10.1371/journal.pone.0052038;
RA   Tang S., Gong Y., Edwards E.A.;
RT   "Semi-automatic in silico gap closure enabled de novo assembly of two
RT   dehalobacter genomes from metagenomic data.";
RL   PLoS ONE 7:E52038-E52038(2012).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CP003870; AFV06266.1; -; Genomic_DNA.
DR   RefSeq; WP_015044301.1; NC_018867.1.
DR   AlphaFoldDB; K4L6N9; -.
DR   STRING; 1131462.DCF50_p2263; -.
DR   KEGG; dec:DCF50_p2263; -.
DR   PATRIC; fig|1131462.4.peg.2280; -.
DR   eggNOG; COG0474; Bacteria.
DR   HOGENOM; CLU_002360_3_3_9; -.
DR   Proteomes; UP000000482; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 2.
DR   Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR   Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 2.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
DR   InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR   InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
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; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01494; ATPase_P-type; 3.
DR   PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR42861:SF156; CALCIUM-TRANSPORTING ATPASE; 1.
DR   Pfam; PF00689; Cation_ATPase_C; 1.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00120; HATPASE.
DR   SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SMART; SM00831; Cation_ATPase_N; 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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Hydrolase {ECO:0000313|EMBL:AFV06266.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000482};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        41..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        69..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        236..257
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        641..664
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        670..691
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        712..737
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        749..768
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        788..807
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        819..839
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..65
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
SQ   SEQUENCE   848 AA;  93140 MW;  8C468E04BC48AAAD CRC64;
     MTEQQIRELQ GLSSSEARQL QERFGKNELV PEKKESFPHK ILQVISEPMF LLLLIAAVIY
     FILGEPRDGA IMLVFVVGII SIEVIQEWKT DQTLRALKDL STPKISVLRD GMMQIINSSD
     LVPGDIMFIA EGVKVPADGT VLKASTLCVD ESSLTGESAG VWKVVYGDKA ANGELSLDSK
     EYWRRDYCYA GTLVTQGTGT IRVDQIGPAT EYGKIGQEIA AAPDRPTPLE KQTGKLVKLC
     AGIAAVLFAL VGVVTYFNLP DHVGSERVIE SILSGITLAM AMIPEEFPVI LTVFLSMGAW
     RLAKKQSLVR RLSSVETLGA VSVLCVDKTG TITMNQMTVR DTWSLNDDGK GLIRIMGMGC
     EPDAYDPMEK AMIAYCEVQG IGRELLFGGE LIKEYAFTDQ TKMMGHVWQN ENELVVAAKG
     SPERILDVCS LTDQERKVAE HKIREMSQQG LRVIAVGQMV LAGKEEVPDT LPECRLQLCG
     MVGLADPPRE SVKQDIQICN KAGVRVVMIT GDNGITASTI ARQINMPNCD KIITGDELNQ
     MSEEELREKV KDVSIFSRVI PEHKMRIVKA FKDNGEIVAM TGDGVNDAPA LKYADIGIAM
     GKRGSEVSRE AADLVLLDDN FSTIVDTIKD GRRIYDNIRK AVGYVFTIHI PIAFASLLAP
     FLGISPASLL LLPLHVVLLE VVIDPTCSIV LERQPAERDI MDQPPRNPNE KLLTAKILSK
     SVLQGLVIFG ASFGTYFTVL NNHPDQASLA RTMALAIILL ANLVLVQVNS SNTDSAFRSF
     AKLIRDKVMW MVNIGTIAGL LLIIYTPLNH LLKLAPLSWK QLILAAALAV VSVGWYEVVK
     GFKRWKRT
//
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