ID A4FGA4_SACEN Unreviewed; 1456 AA.
AC A4FGA4;
DT 17-APR-2007, integrated into UniProtKB/TrEMBL.
DT 17-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE SubName: Full=Cation-transporting ATPase I {ECO:0000313|EMBL:PFG96784.1};
DE SubName: Full=Cation-transporting ATPase, E1-E2 family {ECO:0000313|EMBL:CAM03079.1};
DE EC=3.6.3.- {ECO:0000313|EMBL:CAM03079.1};
GN Name=ctpI {ECO:0000313|EMBL:CAM03079.1};
GN OrderedLocusNames=SACE_3808 {ECO:0000313|EMBL:CAM03079.1};
GN ORFNames=A8924_4195 {ECO:0000313|EMBL:PFG96784.1};
OS Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 /
OS NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharopolyspora.
OX NCBI_TaxID=405948 {ECO:0000313|EMBL:CAM03079.1, ECO:0000313|Proteomes:UP000006728};
RN [1] {ECO:0000313|EMBL:CAM03079.1, ECO:0000313|Proteomes:UP000006728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 /
RC NRRL 2338 {ECO:0000313|Proteomes:UP000006728}, and NRRL 2338
RC {ECO:0000313|EMBL:CAM03079.1};
RX PubMed=17369815; DOI=10.1038/nbt1297;
RA Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S.,
RA Haydock S.F., Leadlay P.F.;
RT "Complete genome sequence of the erythromycin-producing bacterium
RT Saccharopolyspora erythraea NRRL23338.";
RL Nat. Biotechnol. 25:447-453(2007).
RN [2] {ECO:0000313|EMBL:PFG96784.1, ECO:0000313|Proteomes:UP000225825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40517 {ECO:0000313|EMBL:PFG96784.1,
RC ECO:0000313|Proteomes:UP000225825};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (SEP-2017) 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}.
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DR EMBL; AM420293; CAM03079.1; -; Genomic_DNA.
DR EMBL; PDBV01000001; PFG96784.1; -; Genomic_DNA.
DR RefSeq; WP_011874158.1; NZ_PDBV01000001.1.
DR STRING; 405948.SACE_3808; -.
DR KEGG; sen:SACE_3808; -.
DR eggNOG; COG0474; Bacteria.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_002360_0_1_11; -.
DR OrthoDB; 9814270at2; -.
DR Proteomes; UP000006728; Chromosome.
DR Proteomes; UP000225825; 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 GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd00371; HMA; 1.
DR Gene3D; 3.30.70.100; -; 1.
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; 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; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_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; 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; SSF55008; HMA, heavy metal-associated domain; 1.
DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS50846; HMA_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000313|EMBL:CAM03079.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000006728};
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 1391..1411
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1423..1443
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 38..107
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 1456 AA; 150467 MW; F2B4DC8694F2376C CRC64;
MALGRVISAA SQLASPVWDA VRTVVASPSR RRMFAAEDRT HLDVRGLHRP GTEALAGKLE
VLLQDMPGVR SAEVNGVLGR IAITYDPETV TPHELADAIT DFEQRHDLDG RPAQGVKHPG
DAALLLREVG AVGLGIAGLG YAMATSVLPV RALPSLVPVT FSLVGSVPWM RSTAEKAVGR
TFLDTSLAAA GLTSQALAQR PLGLFTDTCE RLCTTREYLA RREAWRRWEQ NAAAGAHRSA
PVEVAPRPVP LPDGAVERVA NTSGALALGG YGAVLAISRL PQRALATLAA GVPRPGSAGR
EAFAAQVASA LSHRGNLVLD PDALRRLDRV DAVVFDAAVL RTGRDVVDTV LGVDPGTDIT
TFVERANELI DPADPRKRER NGAWSTMPLA DCKAALPSHI RDAAREESRR GGTVVVLLHD
SEPVAIASVA PELDPLAEAL VDAARGVGTV AVAGIGGKLG ERLEVDRVVA GGSRLAQSVR
DLQAEGRVVA VVSFRAHSAL LASDVGIGLP DAESRVPWGA HVSCINPAEA HTLLAAVPYA
RRASNYAAAL SVAGSCAGAA FGALGPAATA PSRASMPVQA ATLCALGTGT WTGIQVTHLP
PPSARARTPW HALPVQAVLA LLGTSPRGLD EPEAARRKQP VETDHTEVGV TTATIEGLIN
PMTAVLGVGA AVSAGLGSFL DAGMIMFVLG ASAVVDGVQR VSTNRELAKL LSAGQLPARL
RRDGTTRTVP ADQLVPGDIV ELHAGDGVPA DCRVLEAEGV ELDESSLTGE SQLVAKSPQA
TGATMVADRT SMLYQGTVVA SGRAIAVVVA TGSRTELGST TTQDDGGACS GTGGVEARLS
ALTKRTIPIS AGAGVALAVA DLVRGHPAGQ AISRAVGLAV AAVPEGLPFV ATVAETAAAR
RLADRGVLVR SPKTIEALGR VDALCFDKTG TLTQGRISLR EVSDGRSSRA VEHLDPWLRQ
VVTTAVHASP EPEDDRPLAH PTDQAVVDGA QRAGIGITNA FTVLADLPFE PSRGYHAVRA
AGPGGHRVSV KGAPEVVLGR CVRWLGQDGE RPFDRDARVE IEDEVERLAQ LGYRVLAVAE
RSASPRPELD DDDVADLDFY GLLALADPVH PTAAEAVGRL SRAGVDVIMI TGDHPSTAEA
IAVELDMLRG RRVVNGAELD AMDDDELTSN LPKIAVFARV SPSQKARIVR SLRQGGRVVA
MTGDGANDVP AIKLAQVGIA LGSRATPAAR EAADLVIADD RIETISDAIV EGRGMWASVH
DALSILLGGN LGEIAFTLGA GLLGTAAAPN TRQLLVVNLL TDVLPALAIA VRPPPGATPE
QLLSEGPEVS LGAALNRDVY VRAAATAGAA AAAWLLTRPL ATAGQARTAG LVALVSAQLG
QTMAMRGRTP LVLLAGAASM VVLAGVVQVP GVSQFFGSSP LLAHQWLAAL TAAAVATVAV
WIWQLQSGGE GSATGR
//
