ID G5GCT6_9BACT Unreviewed; 731 AA.
AC G5GCT6;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 63.
DE SubName: Full=Copper-translocating P-type ATPase {ECO:0000313|EMBL:EHG22582.1};
GN ORFNames=HMPREF9332_01387 {ECO:0000313|EMBL:EHG22582.1};
OS Alloprevotella rava F0323.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Alloprevotella.
OX NCBI_TaxID=679199 {ECO:0000313|EMBL:EHG22582.1, ECO:0000313|Proteomes:UP000015993};
RN [1] {ECO:0000313|EMBL:EHG22582.1, ECO:0000313|Proteomes:UP000015993}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0323 {ECO:0000313|EMBL:EHG22582.1,
RC ECO:0000313|Proteomes:UP000015993};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Blanton J.M.,
RA Baranova O.V., Tanner A.C., Dewhirst F.E., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Prevotella sp. oral taxon 302 str. F0323.";
RL Submitted (AUG-2011) 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:EHG22582.1}.
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DR EMBL; ACZK01000023; EHG22582.1; -; Genomic_DNA.
DR RefSeq; WP_009347865.1; NZ_JH376831.1.
DR AlphaFoldDB; G5GCT6; -.
DR STRING; 679199.HMPREF9332_01387; -.
DR PATRIC; fig|679199.3.peg.1541; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_0_3_10; -.
DR OrthoDB; 9770315at2; -.
DR Proteomes; UP000015993; 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 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; 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; TIGR01512; ATPase-IB2_Cd; 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; 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|RuleBase:RU362081};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW Reference proteome {ECO:0000313|Proteomes:UP000015993};
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..117
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 123..139
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 160..182
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 188..206
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 340..362
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 374..402
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 679..698
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 704..726
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 2..68
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 731 AA; 79076 MW; B5D01BE978F59560 CRC64;
MKTETFPVEG LMCANCAMHT ERALKNMEGV ENAVCNFASL EAQVTYDPAR VTPNEMAEAV
EKAGYKLVVL QQQAGAENNV TENIEEMRAQ NFLQAKRRTI MAVLLTTVVT IINIFFVESN
PRLGYPLWLL ATVVVFFAGR QFYINAWKQL QQRTSNMDTL VALSTGIAYL FSIFNLLFPH
VLGKDAHLYF DSSCGIITFI LIGRLLEAHA KANTATSLKK LMGLRPKMTI ILREGRQEEI
EISRVVGGDL LLVRPGEKIP VDGTVVEGSS YVDESLLSGE SVPVLKEQGN KVFEGTLNQK
GSFSFRAEKV GAETMLARII EMVREAQNSK APIQNIVDKV AAIFVPTIIA LAVLSGLLWF
LFGNEPGGNL TRALLSTVTV LVIACPCALG LATPTAIMVG IGRAAEKGIL IKDAESLETA
KHIDTIVLDK TGTITEGRPA LSEPLTALTP EQRSILLSLE NRSEHPLAQA LTASLADAEA
VEITNFQSLT GRGVSGSHNG TTYFVGSERL LKEQAPHLAA QSEEKTDEEA LTTIYFFTPN
ALLATLHIAD RVKASSRAAL KELEQMGIEI HLISGDSEKA TAAMAQMLGI THFRGGVLPK
DKAAYVKQLQ SAGRRTAMVG DGINDSAALA QADLSLAMGK GADVAMDIAQ MTIIQSDLTR
IAEAIRLSRK TTRIIRENLF WAFCYNVTLI PIAAGVLIPI CGFALPPMFA AAAMALSSVS
VVSNSLRLKW A
//
