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Database: UniProt
Entry: A0A367FML5_9ACTN
LinkDB: A0A367FML5_9ACTN
Original site: A0A367FML5_9ACTN 
ID   A0A367FML5_9ACTN        Unreviewed;      1346 AA.
AC   A0A367FML5;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Cation-translocating P-type ATPase {ECO:0000313|EMBL:RCG31092.1};
GN   ORFNames=DQ384_13405 {ECO:0000313|EMBL:RCG31092.1};
OS   Sphaerisporangium album.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Sphaerisporangium.
OX   NCBI_TaxID=509200 {ECO:0000313|EMBL:RCG31092.1, ECO:0000313|Proteomes:UP000253094};
RN   [1] {ECO:0000313|EMBL:RCG31092.1, ECO:0000313|Proteomes:UP000253094}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCTCC AA 208026 {ECO:0000313|EMBL:RCG31092.1,
RC   ECO:0000313|Proteomes:UP000253094};
RA   Li L.;
RT   "Sphaerisporangium craniellae sp. nov., isolated from a marine sponge in
RT   the South China Sea.";
RL   Submitted (JUN-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:RCG31092.1}.
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DR   EMBL; QOIL01000006; RCG31092.1; -; Genomic_DNA.
DR   OrthoDB; 9814270at2; -.
DR   Proteomes; UP000253094; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000253094};
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        1203..1220
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1255..1276
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1288..1307
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          470..541
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          188..254
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          485..511
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1310..1346
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        196..210
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        492..511
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1346 AA;  138895 MW;  2462F4EBA321B3BD CRC64;
     MVTQTLASRP LGLVTQTAGS VCRYVEARAE FGAWKRLEER LAGIPGSYRH IRAVAGPCPD
     HLPHGPIERY AEIAAPASAA AYAATRLITA HGPRALSVLV AGTPKIADVT REAFAGAIGR
     ALAARESVVL NAHVLRAMDR VDTVILHADV LTTGAWTIDR VEPLTEGMTT GELYARLYSL
     IDFSDPGGGT RSGDAASGEF SGTTSGKTPG EANGKAPGKA SGAVNGKASG NGDSADGRSG
     EGEGGDAGQD WSITPIEDLD VLPSTWGPVW RERGLRAFEV RSGGKPIAVA GLAREVDPLA
     EAIVAAAKAA GTVVLAGGQD LAQRFSIKEV LAADADAACH VCGLQARGHG VVVVTRGAGA
     ALAQADIGVG VPDAEGIVPW DADVVADQSG VHLFLSCLPR AVSTSTNGVR LGAAAAVVGS
     LLAIAGPEAT ALRRAYFLDA AASVAAVLLG EWSGRAAGRR PAPLRADATP WHAMSVKEVL
     ARLGSSSHGI SGEEAEGRRR EGGPEEAERP RSLARTMGEE LANPLTPALA AGAVLSALVG
     SVLDAIMISV VMVTNALLGG VQRFRADRAL HRLTEATEVR VRLRRPDGTV AATKEDLAPG
     DVVELRAGDA VPADARVIKA VGLEVDESTL TGESQLVTKT AAPTVAAAVA DRSSMVYQGT
     TVAAGSGRAV IVATGDMTEA GRSARLAGEP SPPTGVELRL RELSRRILPI SIGAGVVLLL
     TDLWRGRPLA AALTPAVSLT VAAVPEGLPF VATLAELAAA RRLSKRAALV RNPSTIEALG
     RVNVLCFDKT GTLTVGHISL RYVSDGQVGA PVEEATERLR RILAAAVRAS PLSGGGRVIA
     HPTDRAVLDG AERIGVTPQE GLESWERVDE MPFEPGRGYH AVLGATERGQ LLSVKGAPEI
     VLTHCDKVLA DGTPVPLDDV ARRALEREVD RLAHQGFRVL AVAERPASDR SDLDESRIEE
     LCFLGFLGLA DPVRPTAAES VRRLVRAGVR IVMVTGDHPS TAEAIAAELD ALNGRRVMTG
     PELEELDDET LTKVLPDVAV FARATPAHKA RIVTCLRRAG EVVAVTGDGA NDAPAIRMAD
     VGIALGSRAT PAARAAADLV VTDDRIETIV DAIVEGRAMW TSVRDSLSIL LGGNVGEVIF
     TVGTGLLAGG SALNARQLLL VNLLTDMAPA LAVAVRPPAS VDPEKLLAEG PEASLGASLT
     RDIYLRSVVT ASAAIAAWLA GRLTGTKGRA DTIGLVALVA AQLFQTVAGG GRDRLVVLAS
     LGSLAMLWLA VSVPGVSRFF GSRPLGPVGW AIGLGCAAAA TGLGALVQRR AAQAPAAPER
     PGDARPEPVP ATHEAEPGRT PSYQQT
//
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