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Database: UniProt
Entry: A0A0K1W170_9MOLU
LinkDB: A0A0K1W170_9MOLU
Original site: A0A0K1W170_9MOLU 
ID   A0A0K1W170_9MOLU        Unreviewed;       959 AA.
AC   A0A0K1W170;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Na(+)/K(+)-exchanging ATPase {ECO:0000256|ARBA:ARBA00039096};
DE            EC=7.2.2.13 {ECO:0000256|ARBA:ARBA00039096};
GN   Name=ctp {ECO:0000313|EMBL:AKX34070.1};
GN   ORFNames=SLITO_v1c04170 {ECO:0000313|EMBL:AKX34070.1};
OS   Spiroplasma litorale.
OC   Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC   Spiroplasma.
OX   NCBI_TaxID=216942 {ECO:0000313|EMBL:AKX34070.1, ECO:0000313|Proteomes:UP000067476};
RN   [1] {ECO:0000313|EMBL:AKX34070.1, ECO:0000313|Proteomes:UP000067476}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN-1 {ECO:0000313|EMBL:AKX34070.1,
RC   ECO:0000313|Proteomes:UP000067476};
RX   PubMed=26430038;
RA   Lo W.S., Lai Y.C., Lien Y.W., Wang T.H., Kuo C.H.;
RT   "Complete Genome Sequence of Spiroplasma litorale TN-1T (DSM 21781), a
RT   Bacterium Isolated from a Green-Eyed Horsefly (Tabanus nigrovittatus).";
RL   Genome Announc. 3:e01116-15(2015).
CC   -!- FUNCTION: This is the catalytic component of the active enzyme, which
CC       catalyzes the hydrolysis of ATP coupled with the exchange of sodium and
CC       potassium ions across the plasma membrane. This action creates the
CC       electrochemical gradient of sodium and potassium ions, providing the
CC       energy for active transport of various nutrients.
CC       {ECO:0000256|ARBA:ARBA00037422}.
CC   -!- SUBUNIT: The sodium/potassium-transporting ATPase is composed of a
CC       catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an
CC       additional regulatory subunit. {ECO:0000256|ARBA:ARBA00038795}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CP012357; AKX34070.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0K1W170; -.
DR   STRING; 216942.SLITO_v1c04170; -.
DR   KEGG; sll:SLITO_v1c04170; -.
DR   PATRIC; fig|216942.3.peg.420; -.
DR   OrthoDB; 9813266at2; -.
DR   Proteomes; UP000067476; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; PTHR43294; SODIUM/POTASSIUM-TRANSPORTING ATPASE SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR43294:SF13; SODIUM/POTASSIUM-TRANSPORTING ATPASE SUBUNIT ALPHA; 1.
DR   Pfam; PF13246; Cation_ATPase; 1.
DR   Pfam; PF00689; Cation_ATPase_C; 1.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 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; 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:UP000067476};
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        49..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        89..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        253..275
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        281..308
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        683..704
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        716..734
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        755..780
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        820..837
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        857..876
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        896..922
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          3..77
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
SQ   SEQUENCE   959 AA;  107203 MW;  4F1416EA40214A84 CRC64;
     MEDYLSSDAK SIQEKYKVSL EEGLSSKQLE ENYKLYGKNE ISTKKQKHWF LIFLKALVEP
     ILLVLLIAAV ISVIAQLLSN DWKVEVEEFI DAFVIVAIVL LDAILETIQT IKARKSTDAL
     KSLSKPIAVV IRNGQQQEIP ASELTIGDIV VLEAGRYVPA DLRIIEQSDL FIDESILTGE
     SIPVAKTHLK ITNNTDILAE MKNIAFMSTF TTNGRAIGIV IKIAKETEIG KISESINNSD
     EELTPLEKKL NKFTYCVAGL SVLIGLLIFI TLFFVGNKGA WVNYLMVGIT LSIGVIPECL
     AAIVSITLSL STKKMASENV IVKKLQAVET LGSVNYICTD KTGTLTQNRM TVKRLIINNS
     IEDVNKFLYK NETHKDFFMK ALVLCNDSIT EGEERIGDPT ELALVDYAEI HKYDEKLARK
     KWKRVFEIPF DSERKMMTTV NLIDDENVVF TKGAIDELLK VCSNIMVNGI VRSITSEDIN
     SMMSLYQELS EHALRVLGFA YKNIKDYNNK NLLEKELTFV AAVAMIDPVR ESAVRAVQQA
     HNAGIRVVMI TGDHASTALA IAKDLDLAQN QTEVLSSDDL NKMDDDQLAK IIEQIKVFAR
     VNPEHKVRIV DALKKHDYIV SMTGDGVNDA PSLAKADIGV AMGITGTDVA KEAADVILTD
     DNFETIIKGV NEGRNVYQKI KRAISFIIGV NLANVLAIFI LSTINTISPL EATNILWMNL
     VVESVIALSI GMGSNDPTLM KVKPIKGKNP ILQGLWFTFA KIIVFLSIAT IGSFYIGMIY
     TTEAEVLALT DNKYTSWYEA LRSSDISYAN KSLIQNHGRL TMFVTITSAP CFFANFIKLS
     NWKSSKKVNV LPNKSLWISS FVSIAINILI IFIPVFNSEV MKLPTLNEYT TKNWYLILFA
     VLISFIPGLA MLILDGIIFF SYHYLPDPWR RNQLISKEFV NEDIKLKKLK KRQKTKNID
//
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