ID   C7M5J6_CAPOD            Unreviewed;       833 AA.
AC   C7M5J6;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   27-MAR-2024, entry version 92.
DE   SubName: Full=Heavy metal translocating P-type ATPase {ECO:0000313|EMBL:ACU91806.1};
GN   OrderedLocusNames=Coch_0243 {ECO:0000313|EMBL:ACU91806.1};
OS   Capnocytophaga ochracea (strain ATCC 27872 / DSM 7271 / JCM 12966 /
OS   NCTC 12371 / VPI 2845) (Bacteroides ochraceus).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Capnocytophaga.
OX   NCBI_TaxID=521097 {ECO:0000313|EMBL:ACU91806.1, ECO:0000313|Proteomes:UP000006650};
RN   [1] {ECO:0000313|EMBL:ACU91806.1, ECO:0000313|Proteomes:UP000006650}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27872 / DSM 7271 / JCM 12966 / VPI 2845
RC   {ECO:0000313|Proteomes:UP000006650};
RX   PubMed=21304645; DOI=10.4056/sigs.15195;
RA   Mavrommatis K., Gronow S., Saunders E., Land M., Lapidus A., Copeland A.,
RA   Glavina Del Rio T., Nolan M., Lucas S., Chen F., Tice H., Cheng J.F.,
RA   Bruce D., Goodwin L., Pitluck S., Pati A., Ivanova N., Chen A.,
RA   Palaniappan K., Chain P., Hauser L., Chang Y.J., Jeffries C.D., Brettin T.,
RA   Detter J.C., Han C., Bristow J., Goker M., Rohde M., Eisen J.A.,
RA   Markowitz V., Kyrpides N.C., Klenk H.P., Hugenholtz P.;
RT   "Complete genome sequence of Capnocytophaga ochracea type strain (VPI
RT   2845).";
RL   Stand. Genomic Sci. 1:101-109(2009).
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; CP001632; ACU91806.1; -; Genomic_DNA.
DR   RefSeq; WP_012797005.1; NC_013162.1.
DR   AlphaFoldDB; C7M5J6; -.
DR   STRING; 521097.Coch_0243; -.
DR   GeneID; 29675082; -.
DR   KEGG; coc:Coch_0243; -.
DR   eggNOG; COG2217; Bacteria.
DR   HOGENOM; CLU_001771_0_3_10; -.
DR   Proteomes; UP000006650; 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; IPR045800; HMBD.
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; PF19335; HMBD; 2.
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   SUPFAM; SSF55008; HMA, heavy metal-associated domain; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 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:UP000006650};
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        178..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        210..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        243..266
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        278..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        434..456
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        462..485
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        779..801
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        807..826
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          1..64
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   833 AA;  89779 MW;  F579C92041010472 CRC64;
     MEYNIEGMGC RGCANTIQKK LSEVAGVTAV TVDFATKKAT VETDREIPFE ALEKALEGTH
     YSIHQASNSE GSGVFYCPMH CEGDKTYDHP GDCPICGMHL VEQVGGAQQQ HHHHEETPKK
     AKGSGVFYCP MHCEGNKTYD HPGDCPVCGM DLVEQVSTEA PEGESAEEQK RKKLRRHFWG
     AVAFTLPIFI IAMIGMWHNN PLYELMPVSA WNWVQFALSL PVVFYFCWIF FERAWRSIRT
     LHFNMFTLIG IGAGVAWLFS VVGLLVPDMF PEQFKEHGSV HLYFEAATVI LTLVLLGQVL
     EADAHSRTQG AIKKLLNLAP NEATKIVHGE EIRVSIEEVT LGDLLRVKPG EKIPVDGVIT
     EGSASIDESM ITGEPIPAEK EVGSKVSAGT LNGAQSFVMK AEKVGSDTLL SQIVQLVQQA
     SSSRPPIQNL ADKIASYFVP IVIGISVLTF VIWSVFGGEN AYVYALLNAV AVLIIACPCA
     LGLATPMSVM VGVGKGAQNG ILIRNAEALE VMNKVNTLVI DKTGTLTEGK PSVSEVFTFG
     NRSEKDLLQV LYSLNQHSEH PLAKATNAYT QAQGATPLSF TNFEALAGRG VKASYEGKNF
     FFGNERLMEE IGAPLSEEIQ TVVKTAQAAG KTVSLLAIEK EIIGVVTITD RVKTSTVQAL
     QELQDLGVEI VMLTGDNSLT AAAIAKEIGI SNYKAGMLPQ NKQAEVARLQ AEGKIVAMAG
     DGINDAPALA QANVGIAMGT GTDIAIESAE ITLVKGDLNG IVKAKKLSKA VMKNIHENLF
     FALVYNVVGI PVAAGVLYPI FGILLSPMLG ALAMSFSSVS VISNALRLRR TKL
//