ID C4F9I2_9ACTN Unreviewed; 791 AA.
AC C4F9I2;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Copper-exporting ATPase {ECO:0000313|EMBL:EEP44506.1};
DE EC=3.6.3.4 {ECO:0000313|EMBL:EEP44506.1};
GN ORFNames=COLINT_02716 {ECO:0000313|EMBL:EEP44506.1};
OS Collinsella intestinalis DSM 13280.
OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales;
OC Coriobacteriaceae; Collinsella.
OX NCBI_TaxID=521003 {ECO:0000313|EMBL:EEP44506.1, ECO:0000313|Proteomes:UP000003295};
RN [1] {ECO:0000313|EMBL:EEP44506.1, ECO:0000313|Proteomes:UP000003295}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13280 {ECO:0000313|EMBL:EEP44506.1,
RC ECO:0000313|Proteomes:UP000003295};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (APR-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}.
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:EEP44506.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ABXH02000014; EEP44506.1; -; Genomic_DNA.
DR AlphaFoldDB; C4F9I2; -.
DR STRING; 521003.COLINT_02716; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_0_3_11; -.
DR Proteomes; UP000003295; 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:0005507; F:copper ion binding; IEA:InterPro.
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; IPR006122; HMA_Cu_ion-bd.
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; 2.
DR NCBIfam; TIGR00003; copper ion binding protein; 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; PR00120; HATPASE.
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 Copper {ECO:0000256|ARBA:ARBA00023008};
KW Copper transport {ECO:0000256|ARBA:ARBA00022796};
KW Hydrolase {ECO:0000313|EMBL:EEP44506.1};
KW Ion transport {ECO:0000256|ARBA:ARBA00022796};
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 Repeat {ECO:0000256|ARBA:ARBA00022737};
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}; Transport {ECO:0000256|ARBA:ARBA00022796}.
FT TRANSMEM 112..133
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 145..162
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 223..241
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 376..398
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 410..432
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 723..745
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 751..770
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 9..75
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 791 AA; 81893 MW; 2F877D9102DE9EB5 CRC64;
MLRKELHLAH QTFDVRGMTC AACQAHVDRA VGNLEGVSNV AVNLLAGSMA VDYDEDAVDA
DAICAAVDRA GYAASPVEVG SNAGTGASAA APRLESPTKK LEAQARAMRG RLIISIAFLI
PLFYLGMGHM LGWPLPAFFG APENIMNVAL TELLLLAPIV YVNDSYFING FKSLIHGAPT
MDALIAIGSA ASIGWSIVGI YRIAAALTAG DPHAAHMVGM DNLYLESAGT ILALVTVGKY
METRSKSKTG GAIERLIDLA PKTATVVGED GMQTTVNADD IQLGQTILVR PGEAIPVDGV
VLEGSSAVDE SALTGESMPV EKRIGDTVSA ATVNRTGSFT FRATRVGADT DLARIIRLVE
DANATKAPIA RLADKVAGVF VPVVLAIAAV TFVVWLIATG GNVNEALTSA VAVVVISCPC
ALGLATPVAI MVGTGRGAEM GILFKSAEAL ETLHDVRAVV LDKTGTITAG KPTVTDVMPA
RRADGSPVMS EKALMKLAAA LERTSEHPLA EAIMARADEL GIVARTVQDF AAIPGRGVTA
REGANAIAAG NAALMDELGV VVDRAALDEL ARAGKTPLLF AKNGELVGII AVADDVKATS
AAAIAALGKL GIRTIMLTGD NETTARAIAA KVGVSEVIAG VMPADKERVV RELQGDGDTV
AMVGDGINDS PALARADVGL AIGAGADVAK EGADVILMKS DLMDVPRAIE LSRAVIRNIK
QDLFWALFYN ALGIPLAAGV FYPLLGWQLS PMFGASAMSL SSLCVVGNAL RLRTFQPRRI
DQPSQLGTGT D
//
