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Database: UniProt
Entry: F8DEA6_HALXS
LinkDB: F8DEA6_HALXS
Original site: F8DEA6_HALXS 
ID   F8DEA6_HALXS            Unreviewed;       912 AA.
AC   F8DEA6;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   SubName: Full=ATPase, P-type (Transporting), HAD superfamily, subfamily IC {ECO:0000313|EMBL:AEH39388.1};
DE            EC=3.6.3.8 {ECO:0000313|EMBL:AEH39388.1};
GN   OrderedLocusNames=Halxa_0145 {ECO:0000313|EMBL:AEH39388.1};
OS   Halopiger xanaduensis (strain DSM 18323 / JCM 14033 / SH-6).
OG   Plasmid pHALXA02 {ECO:0000313|EMBL:AEH39388.1,
OG   ECO:0000313|Proteomes:UP000006794}.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Halopiger.
OX   NCBI_TaxID=797210 {ECO:0000313|EMBL:AEH39388.1, ECO:0000313|Proteomes:UP000006794};
RN   [1] {ECO:0000313|Proteomes:UP000006794}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18323 / JCM 14033 / SH-6
RC   {ECO:0000313|Proteomes:UP000006794};
RC   PLASMID=Plasmid pHALXA02 {ECO:0000313|Proteomes:UP000006794};
RX   PubMed=22675596; DOI=10.4056/sigs.2505605;
RA   Anderson I., Tindall B.J., Rohde M., Lucas S., Han J., Lapidus A.,
RA   Cheng J.F., Goodwin L., Pitluck S., Peters L., Pati A., Mikhailova N.,
RA   Pagani I., Teshima H., Han C., Tapia R., Land M., Woyke T., Klenk H.P.,
RA   Kyrpides N., Ivanova N.;
RT   "Complete genome sequence of Halopiger xanaduensis type strain (SH-6(T)).";
RL   Stand. Genomic Sci. 6:31-42(2012).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CP002841; AEH39388.1; -; Genomic_DNA.
DR   RefSeq; WP_013881929.1; NC_015667.1.
DR   AlphaFoldDB; F8DEA6; -.
DR   GeneID; 10799478; -.
DR   KEGG; hxa:Halxa_0145; -.
DR   eggNOG; arCOG01578; Archaea.
DR   HOGENOM; CLU_002360_3_3_2; -.
DR   OrthoDB; 8588at2157; -.
DR   Proteomes; UP000006794; Plasmid pHALXA02.
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; 2.
DR   PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR42861:SF29; SECRETORY PATHWAY CALCIUM ATPASE, ISOFORM G; 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; PF08282; Hydrolase_3; 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   Hydrolase {ECO:0000313|EMBL:AEH39388.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Plasmid {ECO:0000313|EMBL:AEH39388.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006794};
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        70..88
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        94..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        261..279
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        285..313
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        698..724
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        736..758
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        779..806
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        812..833
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        845..865
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        881..901
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          13..86
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          27..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..49
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   912 AA;  97968 MW;  9BFFE245002051B9 CRC64;
     MTQSDPDTTR ENRWHAMPID AVFGAVSSDE GGLSSAEADR RRSEYGTNDI REAERASPLD
     LFVSQFQNPL IYLLFAAAIL SLGVGVMPGS EPNYAEAAFI GLIIGINGLF GFVQDYQATR
     SIEALRELAS PDATVLRDGR KRSIDAERLV PGDIVYLEQG DAIPADARVL DADELRTNES
     PLTGESTPVA KSSDPVGSDV LLAERSDMVY KNTTVVKGRG SAIVVETGMQ TEVGGIAARL
     GVTADRRTPF QTEVEHLGKQ IGGLVVSLIV LVVAVQFLFT ATEPVAIILV GITLAVAGVP
     EGLPAVVTFT LALGAREMVD RNALVRRLPV VESLGSIDVI VTDKTGTVTE NRMTVTRLYA
     SGAVVDPSDF GSQSADLDVE GRRIATNGDR YSTPAIADVL RCGALCNNAD RIDADEYRGD
     PTEIAIRRAA DEADIEPAAE RIREIPFSSE RKRMTVVVED GGPTAYTKGA PEVVLDRCDA
     ILEDGDVREL TDETRAEILD RTRSFAEDAL RVLAFASKTV SNPSADEDEI EDGMVFLGLQ
     GMIDPPREGV EAAITDCRSA GIRTVLATGD NLTTAAAVGE QIGLDPDGAL EGSDVADRSD
     AELERAVEDI DVFARVTPDH KVSLLNALQS NGHNVVMTGD GVNDAPALTQ ADVGVAMGQR
     GTDVARQASD MILQDDNFAT IRDAIQEGRG IFENVRKFVN YLVSTNTGEV LVVFLGVLLG
     SALFSEQFSG TSQALILTPV LILWINLIAD TLPALAIGAD PHAAGLMDRP PRPADEGVIN
     TRVLASILTI AVLLALTGLG IFFYALDRTG SLVRAQSLLF TFIVVGELIR IQVIRSRYDQ
     TLRSNPWLVG AIVLSFLIHL TVLYTPLHDF FRVVPLTPVD WGWIAVGFLV FLVLNVLVSE
     LNTRIFESRK SD
//
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