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Database: UniProt
Entry: A0A0E3ZJK3_9BACT
LinkDB: A0A0E3ZJK3_9BACT
Original site: A0A0E3ZJK3_9BACT 
ID   A0A0E3ZJK3_9BACT        Unreviewed;       757 AA.
AC   A0A0E3ZJK3;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   SubName: Full=Copper transporter {ECO:0000313|EMBL:AKD05710.1};
GN   ORFNames=PKOR_13300 {ECO:0000313|EMBL:AKD05710.1};
OS   Pontibacter korlensis.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Pontibacter.
OX   NCBI_TaxID=400092 {ECO:0000313|EMBL:AKD05710.1, ECO:0000313|Proteomes:UP000033109};
RN   [1] {ECO:0000313|EMBL:AKD05710.1, ECO:0000313|Proteomes:UP000033109}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=X14-1T {ECO:0000313|EMBL:AKD05710.1,
RC   ECO:0000313|Proteomes:UP000033109};
RX   PubMed=26057562; DOI=10.1038/srep10929;
RA   Dai J., Dai W., Qiu C., Yang Z., Zhang Y., Zhou M., Zhang L., Fang C.,
RA   Gao Q., Yang Q., Li X., Wang Z., Wang Z., Jia Z., Chen X.;
RT   "Unraveling adaptation of Pontibacter korlensis to radiation and
RT   infertility in desert through complete genome and comparative
RT   transcriptomic analysis.";
RL   Sci. Rep. 5:10929-10929(2015).
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; CP009621; AKD05710.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0E3ZJK3; -.
DR   STRING; 400092.PKOR_13300; -.
DR   KEGG; pko:PKOR_13300; -.
DR   PATRIC; fig|400092.3.peg.2901; -.
DR   HOGENOM; CLU_001771_0_3_10; -.
DR   Proteomes; UP000033109; 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; cd00371; HMA; 1.
DR   CDD; cd02094; P-type_ATPase_Cu-like; 1.
DR   Gene3D; 3.30.70.100; -; 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; IPR017969; Heavy-metal-associated_CS.
DR   InterPro; IPR006121; HMA_dom.
DR   InterPro; IPR036163; HMA_dom_sf.
DR   InterPro; IPR027256; P-typ_ATPase_IB.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_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; PF00403; HMA; 1.
DR   Pfam; PF00702; Hydrolase; 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; SSF56784; HAD-like; 1.
DR   SUPFAM; SSF55008; HMA, heavy metal-associated domain; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
DR   PROSITE; PS01229; COF_2; 1.
DR   PROSITE; PS01047; HMA_1; 1.
DR   PROSITE; PS50846; HMA_2; 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|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU362081};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033109};
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        114..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        139..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        174..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        204..223
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        357..379
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        391..417
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        703..722
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        728..750
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          23..89
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   757 AA;  81717 MW;  BCDA3EFDD88FF935 CRC64;
     MGRIFVIDKT MKEMATVKDK KFTKATFPVE GMTCASCANS IQSMLRTREG VAEADVNFAG
     KTLQVAYDER EVSPAQLRET VQEIGFDILI EEKTQEELEE RQAQALAKLK RKTIIAGVLA
     LPVFVLGMFF HSAFAWGNWA MLILTAPVLL WAGQRFFVGA WLQAKHFRAN MDTLVALSTG
     IAFVFSVFNT VYPEFFISRG LMPHVYYEAV AVIIAFILLG KYLEENAKDR SSSAIKKLMG
     LQPKTVRVLR GNTEMKLKVE EVQLGDRVVL LPGERVPVDG EVAAGSTYVD ESMLSGEPLP
     VQKNPGDTLY AGTINQKGSV QLVAQKTGGE TMLAHIIRLV QEAQGSKAPV QKLVDKIAGI
     FVPVVLVIAL LTLAAWLVFG GEAYLTEALL STISVLVIAC PCALGLATPT AIMVGVGRGA
     ENGILIKDAE SLEHAHKVNA VILDKTGTIT LGKPSVTDVV WAQDMAAKEQ LETLFFSMEA
     QSEHPIAQAI YNFYKEKGQQ ATPLDSFNSL TGLGIEATYN GERYLAGNEK LLRQQGVALP
     EHLLQAARQL QEDAKTAIFF ADGAQALAVF AVSDPIKPAA AEGIKAMQEA GLEIYMLTGD
     NRQTAEAVAR QVAVAHYQAE LLPTDKADFV KKLQAEGKVV AMVGDGINDA QALATADVSI
     AMGQGTDVAM EVAGITLMRS DLTQVAKAVK LSRATVQTIH QNLFWAFFYN VICIPVAAGV
     LFPFTGFLLS PMVAGAAMAL SSVSVVANSL RLRAKNI
//
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