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Database: UniProt
Entry: A0A101IBF1_9CHLR
LinkDB: A0A101IBF1_9CHLR
Original site: A0A101IBF1_9CHLR 
ID   A0A101IBF1_9CHLR        Unreviewed;       745 AA.
AC   A0A101IBF1;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Cation-transporting ATPase {ECO:0000313|EMBL:KUK92161.1};
DE   Flags: Fragment;
GN   ORFNames=XE06_1346 {ECO:0000313|EMBL:KUK92161.1};
OS   Anaerolineaceae bacterium 46_22.
OC   Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae.
OX   NCBI_TaxID=1635294 {ECO:0000313|EMBL:KUK92161.1, ECO:0000313|Proteomes:UP000054480};
RN   [1] {ECO:0000313|Proteomes:UP000054480}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA   Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA   Andersen G.L., Banfield J.F.;
RT   "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT   Other Microbial Community Members in Biogeochemical Transformations in Oil
RT   Reservoirs.";
RL   MBio 7:e01669-15(2015).
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:KUK92161.1}.
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DR   EMBL; LGHA01000196; KUK92161.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A101IBF1; -.
DR   Proteomes; UP000054480; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
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; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01494; ATPase_P-type; 2.
DR   PANTHER; PTHR24093; CATION TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR24093:SF506; CATION-TRANSPORTING ATPASE PMA1; 1.
DR   Pfam; PF13246; Cation_ATPase; 1.
DR   Pfam; PF00689; Cation_ATPase_C; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00120; HATPASE.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        46..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        88..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        532..557
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        604..626
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        674..692
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        712..730
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          556..728
FT                   /note="Cation-transporting P-type ATPase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00689"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KUK92161.1"
SQ   SEQUENCE   745 AA;  81233 MW;  96C7A6D64FAED45B CRC64;
     VNYGRGKGVV VSTGMNTQLG MIATMLQQVE DEQTPLQQRL DQLGKVLGWG SLIVCGLVFV
     IGVARYALQP GAANFFSAEA LETYTELFMV AVSLAIAAVP EGLPAVVTIS LALGMREMVR
     RHALIRKLSS VETLGSATVI CSDKTGTLTQ NEMTVTRIWA DGNFVGVTGS GYTPKGDFTN
     DGKTISLNDF PAVKTALWIG SLNNDAQLEP SGEQAGQETY RMIGDPTEGS ILVAAHKAGC
     SARAINKGFP REQEIPFDSV RKRMVTIHSV QESEGECLSP LDQEDEEKRE WYIVTVKGAP
     DVVLDLCSDM QTINNGNVEL TEDRRKEILA ANDEMTGDAL RVLGVAYRMV PVLPDEINSD
     ELEKDLTFVG LIGMIDPART EVSDALNIAR DAGIRTIMIT GDYPNTARAI AEEIGLLRSG
     RKVMTGSELN HLSDDEMITN VMETDVYARV SPEHKMRIVD ALRANQEVVA MTGDGVNDAP
     AIKRADIGVA MGITGTDVAK GTADMVLTDD NYASIVSAVE QGRVIYSNIR KFVYYLLSCN
     AAEIMIIFLA TLFGWPIPLT AIQLLWLNLV TDGAPALALG TEPGDPDIMD RPPRPSQEPI
     INKYMLIGIV VQTIAITAVT LGAFAIGRFI DPENIEFAET MAFVTLSISE LFRAYTARSE
     FYPLLKIGFF KNKLMNWAVL GSLVLIMLVI YVPFLQPIFN TAPLGLEQWL EILPLVLIPS
     VAAELTKNVI RKMMAKDNRL ETEPV
//
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