ID A0A1M3Q433_9PROT Unreviewed; 878 AA.
AC A0A1M3Q433;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=ATPase {ECO:0000313|EMBL:OJY74302.1};
GN ORFNames=BGP12_20055 {ECO:0000313|EMBL:OJY74302.1};
OS Rhodospirillales bacterium 70-18.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales.
OX NCBI_TaxID=1895826 {ECO:0000313|EMBL:OJY74302.1, ECO:0000313|Proteomes:UP000184399};
RN [1] {ECO:0000313|EMBL:OJY74302.1, ECO:0000313|Proteomes:UP000184399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-18 {ECO:0000313|EMBL:OJY74302.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:OJY74302.1}.
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DR EMBL; MKWE01000015; OJY74302.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M3Q433; -.
DR STRING; 1895826.BGP12_20055; -.
DR Proteomes; UP000184399; 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; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR42861:SF156; CALCIUM-TRANSPORTING 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 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 64..83
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 253..270
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 276..304
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 676..697
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 703..725
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 753..771
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 777..796
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 816..833
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 845..866
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 10..84
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 878 AA; 91859 MW; 87CF0DE48E7E1834 CRC64;
MADTPARVPP WHAMGAAAVL RQLGADTARG LTEAAAAGLL AEHGPNAIRE RTARGPWRMA
LGQFTNFMTL ILIAAALVAG LVGEAGDTIA IVAIVALNAV VGFIQEYRAA NTLASLRRMA
AGQATVVRGG VAQSVSAAAL VPGDIVLLEA GNAIPADLRL IEVHALKLGE AALTGESVPV
EKSSGPLAET ELTLGDRTNM AYKGTAVLFG RGRGVVVATG MATELGRIAG MLAETPETLT
PLQRRLSVLG RHLALAAVAI CVVILAIGIL RGEPPLHMLL TALSLAVAAI PEALPAVVTV
LLALGARRMV QANALIRRLP AVETLGSVSV ICSDKTGTLT ENRMQATEAV LWSGRQEVAA
LDGARMPDAR LLEAMALCSD VAPGRDGAPN GDPTELALWQ AARAAGHDGT VLAAATPRVM
EMPFDSERMR MTTFHRAPAG LVAYTKGAPE VVLARCARVA TVDRTAPCDP AQMLQAAHRM
ADDGLRVLAF AFRHWDSLPA ADDAEAEQDL TLLGLIGLID PPRPEARAAV ATCNAAGIVP
VMITGDHPAT ALAVARALGI AGPTDHATTG SALAAMPDDE LARKVAGLRV YARVDPAQKI
RIVAALQHGG ALVAMTGDGV NDAPALARAD IGVAMGRGGT DVARDAASLV LLDDNFATIV
VAVHEGRRIY DNIRKFVRYA VTCNSAEIWT IFLAPFLGLP VPLLPIQILW INLVTDGLPG
LALAAEPAER LTMQRPPRPA QESMFARGMG RHIIWVGLLM AGIALLTQVV AMGQGPAHWQ
TMVFTVLTLS QLGHVLAIRS ERDSLFRQGV MTNKPMLLAV LVTVALQMAV VYAPPLNAIF
GTEPLSVIEL AGCFALSSIV FIAVEIEKLV LHPARSPK
//
