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Database: UniProt
Entry: C4RDT5_MICS3
LinkDB: C4RDT5_MICS3
Original site: C4RDT5_MICS3 
ID   C4RDT5_MICS3            Unreviewed;       657 AA.
AC   C4RDT5;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   SubName: Full=Heavy metal translocating P-type ATPase {ECO:0000313|EMBL:EEP70021.1};
GN   ORFNames=MCAG_00348 {ECO:0000313|EMBL:EEP70021.1};
OS   Micromonospora sp. (strain ATCC 39149 / NRRL 15099 / SCC 1413).
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=219305 {ECO:0000313|EMBL:EEP70021.1, ECO:0000313|Proteomes:UP000010307};
RN   [1] {ECO:0000313|Proteomes:UP000010307}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39149 / NRRL 15099 / SCC 1413
RC   {ECO:0000313|Proteomes:UP000010307};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Microbial Sequencing Center;
RA   Fischbach M., Godfrey P., Ward D., Young S., Kodira C.D., Zeng Q.,
RA   Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chen Z., Engels R.,
RA   Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.I.,
RA   Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D.,
RA   Pearson M., Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C.,
RA   Sykes S.N., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA   Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA   Galagan J., Nusbaum C., Birren B.;
RT   "The genome sequence of Micromonospora carbonacea var. africana strain ATCC
RT   39149.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
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; GG657738; EEP70021.1; -; Genomic_DNA.
DR   RefSeq; WP_007071301.1; NZ_GG657738.1.
DR   AlphaFoldDB; C4RDT5; -.
DR   STRING; 219305.MCAG_00348; -.
DR   eggNOG; COG2217; Bacteria.
DR   HOGENOM; CLU_001771_6_3_11; -.
DR   Proteomes; UP000010307; 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; TIGR01525; ATPase-IB_hvy; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 1.
DR   PANTHER; PTHR43079:SF1; CADMIUM_ZINC-TRANSPORTING ATPASE HMA1, CHLOROPLASTIC-RELATED; 1.
DR   PANTHER; PTHR43079; PROBABLE CADMIUM/ZINC-TRANSPORTING ATPASE HMA1; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00941; CDATPASE.
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   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:UP000010307};
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        30..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        256..275
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        287..307
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        598..616
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
SQ   SEQUENCE   657 AA;  68869 MW;  7483D4EDA2552CB7 CRC64;
     MTLDERLRTA LPTTPQPRPG ASWWWSLPEI RWATIATGFF ALGLATQLLG APAWAWWACY
     LACYAAGGWE PGWAGLQALR ERRLDVDLLM VVAAIGAAAI GQVLDGALLI VIFATSGALE
     AAATRRTEDS VRRLLDLAPE RANRLADAGE ETVDAADLRV GDVIVVRPGE RIGADGHVID
     GRSEVDQASI TGEPLPADKQ SGDEVFAGTV NGTGALQVRV ARPAADSVVA RIVALVEQAS
     ATKARVQLFI EKIEQWYSIG MVAATLALFV IPLLAGAELT PTLLRAMTFM IVASPCAIVL
     ATMPPLLSAI ATAGRHGVLV KSAVVMERLA TITRVAFDKT GTLTEGRPHL TTVRVLPDTE
     LSEHELLALA AAAEDPSEHP LAGAIVAAAR SRGLTLRPAC DFSSSPGRGV TALVDARTIQ
     VGSAHRLLDD TVTDQTLRQN THAAVTALER DGETAVLVLV DGRPAAVLGL TDRVRPGARP
     TVDALNALTT ATPILLTGDN ATAAARIAAD TGISEVHADL LPEQKVDQVQ RQNTAGHRLL
     LVGDGVNDAP ALAAAHVGIA MGRSGSDLSV ATADAVIVRD DLTAIPAVMN LARRARRLVI
     ANLIIAATFI AVLVGWDLFG HLPLPLGVAG HEGSTVIVGL NGLRLLRNTA WRPVPTA
//
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