ID A0A1J4PSP4_9ACTN Unreviewed; 1320 AA.
AC A0A1J4PSP4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=ATPase {ECO:0000313|EMBL:OIK23941.1};
GN ORFNames=VT52_030130 {ECO:0000313|EMBL:OIK23941.1};
OS Streptomyces malaysiense.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1428626 {ECO:0000313|EMBL:OIK23941.1, ECO:0000313|Proteomes:UP000034838};
RN [1] {ECO:0000313|Proteomes:UP000034838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUSC136T {ECO:0000313|Proteomes:UP000034838};
RA Lee L.H., Chan K.-G.;
RT "Genome sequencing of Streptomyces sp. MUSC136T.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OIK23941.1, ECO:0000313|Proteomes:UP000034838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUSC136T {ECO:0000313|Proteomes:UP000034838};
RA Lee L.-H., Ser H.-L.;
RT "Genome sequence of Streptomyces malaysiense MUSC 136.";
RL Submitted (OCT-2016) 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:OIK23941.1}.
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DR EMBL; LBDA02000086; OIK23941.1; -; Genomic_DNA.
DR RefSeq; WP_063888365.1; NZ_LBDA02000086.1.
DR Proteomes; UP000034838; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 2.
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; 2.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
DR InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
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 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 Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000034838};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 1151..1301
FT /note="Cation-transporting P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00689"
FT REGION 592..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 646..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1320 AA; 136228 MW; 2962B26C375E893E CRC64;
MLFAYWDDGL ARLVVSATEE EATDEVVEHA ARLAARHGLE LAAGDVEEST HPADPAGVRT
AVATFGVDAL GTAVAVTGYA LRLPPSPRLL TAVVTLLREN PRFRAWLRAR LGPDRMDLVL
ATANAAAHGA GQTPASLLLD GTLRACQIAE TVARAVAFDA VHDELCAPDR VSLAPGAEPR
PPLRESPAQE YASHASAGSL LGAAATLLVK HDGTEAAEAV LAGSPKAARY GPAAFHAVLG
AALSRTGVLV RDPERLRRLD LAGTVVLHAG ALRGADGEAD PWAEPVLDAA RRAGLRVVLV
DDPALEDFTG LADQVVDARR PLDDVVHEAR GETHTVLTVA RVRSAEESDV LAALRASDVA
VALTDRDGAV VWGADMLALH GLPDVWRVLI AIPAARAVGG RSQTLARSGA ALSGLLVAVG
EAKGGRGRLA VLPGLRHAPV DVGAAVALLS GMRAALGVAV ARAPHPRPRV HWHELDPEQT
RDRLEHRPEA VRTPLGALAE GLREAADGVS RHPLVAPVRW SYQLGQAVRG ELHDPLTPVL
AVGSAASAIL GSAVDALLVV GALDLNALVG GVQRLRAERA LSGLVADQKR KARLVPPEEE
APAGGTRTVE AGKLTPGDVI QLKGDDVVPA DARLLWQEGL EVDESALTGE SLPVEKDTDP
TPHAPVADRS CMVFEGTTVV AGEARAVVVG TGEHTEAARA VHLAARMPPA AGVQARLQEL
TRKALPLTLA GGAAVTGIAL LRGTPIREAV SGGVAVAVAA VPEGLPLVAT VAQLAAARRL
SRGGVLVRTP RTLEALGRMD TICFDKTGTL TENRLRLVRV SDAEGTVRAV AAAGSAGTVR
AAARACPRFN GGSERPVHAT DEAVLDAARP DPDWIQLAGL PFEAARGYAA AVGRTGDGSR
VLVVKGAPET VLPACTGLPA GAADAAQELA GSGLRVLAVA ERRLGDGEDE AEVLEQPLQE
LEFTGVLALS DVPRETSTAL VKGLLEAGVR PVVLTGDHPQ TARAIAAELG WPEGTVVVTG
DELAAANRAA RARMLRDAGV VARVAPEQKL QVVEALRDAG RVVGMVGDGA NDAAAIRAAD
IGVGISARGS AAARNAADIV LTDDDLTVLI DAVGEGRALW HSVADAIAIL IGGNAGEVGF
GLIGTLVSGR APLSTRQMLM VNLFTDLFPS MAVAVTEKEG EADLAHVEEA AGVLGDPLLR
QIRHRALTTC LGALTAWLIG RFTPGTDRRS STMALCGVVG TQLVQTLLDR RDSRLVQITS
LGSAAVLVAV VQTPVLSRAF GCTPLGPVAW GGVAVAIALA LAGQRALPRL EETVVRLLPA
//
