ID I4C2J8_DESTA Unreviewed; 981 AA.
AC I4C2J8;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=P-type ATPase, translocating {ECO:0000313|EMBL:AFM23789.1};
GN OrderedLocusNames=Desti_1075 {ECO:0000313|EMBL:AFM23789.1};
OS Desulfomonile tiedjei (strain ATCC 49306 / DSM 6799 / DCB-1).
OC Bacteria; Thermodesulfobacteriota; Desulfomonilia; Desulfomonilales;
OC Desulfomonilaceae; Desulfomonile.
OX NCBI_TaxID=706587 {ECO:0000313|EMBL:AFM23789.1, ECO:0000313|Proteomes:UP000006055};
RN [1] {ECO:0000313|Proteomes:UP000006055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49306 / DSM 6799 / DCB-1
RC {ECO:0000313|Proteomes:UP000006055};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Zeytun A.,
RA Lu M., Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "Complete sequence of chromosome of Desulfomonile tiedjei DSM 6799.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP003360; AFM23789.1; -; Genomic_DNA.
DR RefSeq; WP_014808942.1; NC_018025.1.
DR AlphaFoldDB; I4C2J8; -.
DR STRING; 706587.Desti_1075; -.
DR KEGG; dti:Desti_1075; -.
DR eggNOG; COG0474; Bacteria.
DR HOGENOM; CLU_002360_3_0_7; -.
DR OrthoDB; 9759222at2; -.
DR Proteomes; UP000006055; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IPR004014; ATPase_P-typ_cation-transptr_N.
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; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01494; ATPase_P-type; 3.
DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR42861:SF156; CALCIUM-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF00122; E1-E2_ATPase; 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 SMART; SM00831; Cation_ATPase_N; 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; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000006055};
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 65..85
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 91..110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 259..286
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 306..331
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 753..776
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 782..802
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 830..854
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 874..896
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 917..943
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 955..974
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 16..90
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 981 AA; 105610 MW; 8805BAB78D8629E8 CRC64;
MTAGTTNKEQ VPSAQAWHSQ TAEDCAKVLS VHLQQGLSRK VVAKRLKEIG PNELKEMPRP
PFWRLVLEQF QNFVVMMLVV ASIISACLGD YVEAAAIMAI VLLNAIIGVV QESKAEEALA
ALKKMTAPNA LVIRGGTRET VASRDLVPGD IVVLEAGNYV PADLRLIQAI NLQIDEAALT
GESVPVEKDA QVCLEPDIPL GDRHNTAFMG TLITYGRGLG IVIATGMHTQ MGLIATMLQT
LEAEPTPLQQ RLDQLGKQLG YACLAICGLV FVVAVFNQTK LSMIFAPDGG FLQYLRTFST
VLTETFMVAV SLAIAAVPEG LPAVVTVTLA LGMREMIKRH ALIRRLAAVE TLGSASVICS
DKTGTLTQNQ MTTVRLWVDE HAFAITGKGY EPRGDFSLNG ETVDLKEYPA ALTALWSSVL
ASDAYIEPSG SSDESETYRI IGDPTEGALV VAAAKVGAVK TELEICYPRV CEVPFDSERK
CMSTVMSMSN PSPLGALGAN VFQVAPGENG NLYVTACKGA PDVIMQLCTH YLRIDNQPAP
LTDKMRQRMF EANESMAREA LRVLAVAYRI TDSPPAEVKA STIEHSLVFL GLFGMIDPAR
PEVLPAIAKA RTAGIRTIMI TGDYPDTAAA IGSTIGLLET GHGVLSGAAL DRLDEAGMAK
ALETTDVFAR VNPEHKMRIV DGLKSRGEVV AMTGDGVNDA PALKRSDIGV AMGITGTDVA
KETADMVLTD DNYVSIVSAV EQGRIIYANI RKFVFFLLSS NVAEIMIIFL PTLFALPSPM
TAIQLLWLNL VTDGAPALAL AMEKGDPDIM EQQPRPKSEP IIHGPMRLGI IVQTIAQTGA
TLTAFVIGLV WHLSESNAVP AGVNPLSHVF NLNWTGVDVI TAETMAFVTL SLCELFRAFT
VRSERLSLFQ IGPFSNPYLI AAVLGSVAVL LMTVFVPFLN PIFNTTPLTL NEWTVVLGLA
LIPAVTEEFT KLYLRMKERT A
//
