ID H8Z288_9GAMM Unreviewed; 907 AA.
AC H8Z288;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=P-type ATPase, translocating {ECO:0000313|EMBL:EIC22650.1};
GN ORFNames=Thi970DRAFT_02928 {ECO:0000313|EMBL:EIC22650.1};
OS Thiorhodovibrio frisius.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thiorhodovibrio.
OX NCBI_TaxID=631362 {ECO:0000313|EMBL:EIC22650.1, ECO:0000313|Proteomes:UP000002964};
RN [1] {ECO:0000313|Proteomes:UP000002964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=970 {ECO:0000313|Proteomes:UP000002964};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Vogl K., Liu Z., Overmann J.,
RA Frigaard N.-U., Bryant D.A., Woyke T.J.;
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EIC22650.1, ECO:0000313|Proteomes:UP000002964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=970 {ECO:0000313|EMBL:EIC22650.1,
RC ECO:0000313|Proteomes:UP000002964};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Zhang X., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Vogl K., Liu Z.,
RA Overmann J., Frigaard N.-U., Bryant D., Woyke T.;
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; JH603169; EIC22650.1; -; Genomic_DNA.
DR RefSeq; WP_009149622.1; NZ_JH603169.1.
DR AlphaFoldDB; H8Z288; -.
DR STRING; 631362.Thi970DRAFT_02928; -.
DR eggNOG; COG0474; Bacteria.
DR HOGENOM; CLU_002360_3_3_6; -.
DR OrthoDB; 9814270at2; -.
DR Proteomes; UP000002964; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0015662; F:P-type ion transporter activity; IEA:UniProt.
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; PTHR43294:SF22; P-TYPE ATPASE; 1.
DR PANTHER; PTHR43294; SODIUM/POTASSIUM-TRANSPORTING ATPASE SUBUNIT ALPHA; 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; PR00121; NAKATPASE.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 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:UP000002964};
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 58..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 274..298
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 682..707
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 719..737
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 757..782
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 794..818
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 839..859
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 871..890
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 2..74
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 907 AA; 98090 MW; D4B36EC453F03EEC CRC64;
MLWYQLPPKD VLSTLETDDQ GLSSAEATKR QATWGENAIS VRKTPAWERF LKQFKDPMSM
ILLATAMVTG LLTLFGAHLL PDTMVILSVV VLNACVGFYL EGKAENAIEA LKSMMVPECM
VLRDQGLVRI PSKGLVPGDI VELEGGDKIP ADVRFIRLHN AQVDESSLTG ESVPVTKTTN
AIEGDQVVPG DQKNMGFSGT YLTQGTAKAV VVEIGDKTVF GEIAGMVKAA AAHSTPLQRK
LARFIKTLIV AIMSIGAVNF IVGIYLGYEI SYSLLGAISL VVAAIPEMLP ALVTAVLAKS
GNAMARQNAI VANLPAAETL GATSVICSDK TGTLTENRMT VTDVFAAGQA YGVSGVGYDL
HGQFSQDGAP IDAAANPALR RMLEIGFFCN NAHLNDEGHS IGDPTEIALL ISGAKAALNK
DRQQRVEEIP FDSSTKYMAV LTDYEGERYI FVKGAPEILL EMCTSATDAE AKETELNREA
YLEAARTFAR QALRTLGFAF KRVANDHADL LHEDLHDLCF AGLQGMIDPP KESAKQAVAN
CKSAGIRTVM VTGDHPLTAQ AVAGQLGIPA ERVLAGTELN DMDSERLRRE VEEVSVFARV
APEHKQQIAA AFQANGHVVA MTGDGVNDAP ALKQADIGVA MGQEGTEVAR QAADMVLADD
NFATIITAVE EGRHAWKNLQ KAILYTLPTN AAQALLIMGA ILLAAFVPLF GERFVLEPIQ
ILWINLLDSL LLTLPLMMEP KERGLLTHPP RDSKANIIDG LFIQRVILLG IAISLPGFGI
YYLFGSPAVV NGELINPLLL TQAQTAAFWA ILFAHFGYVF SARSIDQSVF SFSPFSNKWL
LAGVGLSIAI RLIPTFAPAT SSWFKTADFP VIWWPVILLC FLPSLLAIEA DKYLRQAWKR
LRPRRGF
//
