ID A0A2S4YE02_9ACTN Unreviewed; 1466 AA.
AC A0A2S4YE02;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Cation-transporting P-type ATPase N-terminal domain-containing protein {ECO:0000259|SMART:SM00831};
GN ORFNames=C3488_24915 {ECO:0000313|EMBL:POX46940.1};
OS Streptomyces sp. Ru72.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2080747 {ECO:0000313|EMBL:POX46940.1, ECO:0000313|Proteomes:UP000237426};
RN [1] {ECO:0000313|EMBL:POX46940.1, ECO:0000313|Proteomes:UP000237426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ru72 {ECO:0000313|EMBL:POX46940.1,
RC ECO:0000313|Proteomes:UP000237426};
RA Suneja G., Sharma R.;
RT "Genome sequencing of cellulose degrading bacteria.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00001836};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {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:POX46940.1}.
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DR EMBL; PQSR01000060; POX46940.1; -; Genomic_DNA.
DR OrthoDB; 9814270at2; -.
DR Proteomes; UP000237426; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma 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 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:SF31; PLASMA MEMBRANE ATPASE-RELATED; 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; 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 PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000237426};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 613..682
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 232..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1466 AA; 150351 MW; 8C8F89DB98553699 CRC64;
MALPGGRLLR SVVSSATASL WDGTRTRVRR FEGRLHIAVR GLSHGELPHA SAARLAEEVE
RRLTGVPGVT WAVANTVLGH AVVGTDDSFD PEELVPALID VVEELEEAHG LEHPLPDHPA
SGRTTRRASL AVAVQVAAAP LAAVTGLARR APLPSSVTAL IPLVDVHPRL RAVVDRAIGT
DNANVLLPLL GAVGHAGSGG VVGVVVDTVR HTLRVLEANA EAAAWAAAEP RLAGSPTTGS
HGPVPAPPPR ETPLRPGAVE RYADQAVLVA AASFAGSLLV TRRPARAAGG ALAAIPKAPL
LAREGFACAL GRGLARRGVL VADSGALRRL DRIGTVLLDT GVLATGSHVL ADLVPLDDDA
PVGDLAARAH RLFDGSAPGK PARDGEWALG PVEHLSVQGR TGARERERMH RDGARLVLGL
AHGRRLLAVI SAVPQMHDAA GAFVPAAHAA GLRVVVAGAH TADPAVREAH AVRAADERLV
DCVRDLQRDG EGVLLISRDR AALSAADVGV GVVGPEGSPP WGAHLYVDAA AAAVVIVRAC
RGARDSARRG VRIAEAAAAV GATAALAGRS GRPAARGVTA FNAAGALATC TGVWSAVRVL
RRPSPVTAAS RRPWHAMDPG TVLERTGSAE AGLTDEEAQA RGTAPGERAP TSSPVRAYLT
EMANPLTPVL GAGAAMSASV GAVLDAVVIV AVTAVSGLVG GFQRYRTDRA VARLRRESGV
MARVLRDERE TTVPAHKLVV GDVVVLSAGD VVPADARLLE AHHLETDESA LTGESLPVAK
AVAPVLASDV AERTSMVYEG TTVAAGRCRA VVVATGTETE ASRAAVLGRG AAMPAVGVER
RLARITRGTL PVALGSAAAV MVAGTLRGRS TRETVGAGVG LAVASVPEGL PFLVSAAQLA
SARRLSARGA LVRDPRTIEA AGRTDVLCFD KTGTLTHGRI SLVAVSADGE SRSLESLGDE
QRAVLAAALR ATPHPHGGAG FEHATDGAVT AGAHEAGVRR TTDVPGWRRV SGLPFEPSRG
FHATMGRIGE RRILSVKGAP EEVVERCATR GGRPLDERER ADVLSAGEKL AAEGHRILAV
AELREAAGEE LRDETVRGLD FVGFLAFADR VRGTAAEAVR HLVESGVHIV MITGDHPGTA
GAMASELGVL DGRRVVTGTE LDDLDDRALD ALLPDVGVVA RGTPVHKVRV VQAFQRLGRT
VAMTGDGAND APAIRLADVG IAFGTRATPA ARAAADLVVT DDRLETVLAA LVEGRAMWAS
VRQALAILVG GNLGEIAFTL LGAAATGTSP LTARQLLLVN LFTDLAPAMA VALRPPRPEA
AERMLHEGPE VSLGTALTEE TVCRAVATAL GATAAWIVAR FTGRAVRART VALVALVGTQ
LGQTLLAGGR SGAIVGSSLG SLAALAAVVQ TPVLSQFFGC TPLGPFAWGI ALSTAAAATV
SSLFLPPLVG RIRAALPRPL PAVAGA
//