ID A0A379JJ50_9NOCA Unreviewed; 931 AA.
AC A0A379JJ50;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Probable cation-transporting ATPase F {ECO:0000313|EMBL:SUD48434.1};
DE EC=3.6.3.- {ECO:0000313|EMBL:SUD48434.1};
GN Name=ctpF_2 {ECO:0000313|EMBL:SUD48434.1};
GN ORFNames=NCTC1934_05769 {ECO:0000313|EMBL:SUD48434.1};
OS Nocardia otitidiscaviarum.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=1823 {ECO:0000313|EMBL:SUD48434.1, ECO:0000313|Proteomes:UP000255467};
RN [1] {ECO:0000313|EMBL:SUD48434.1, ECO:0000313|Proteomes:UP000255467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC1934 {ECO:0000313|EMBL:SUD48434.1,
RC ECO:0000313|Proteomes:UP000255467};
RG Pathogen Informatics;
RA Doyle S.;
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}.
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DR EMBL; UGRY01000005; SUD48434.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A379JJ50; -.
DR STRING; 1406858.GCA_000710895_03995; -.
DR OrthoDB; 9814270at2; -.
DR Proteomes; UP000255467; 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 CDD; cd02080; P-type_ATPase_cation; 1.
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:SF29; SECRETORY PATHWAY CALCIUM ATPASE, ISOFORM G; 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 Hydrolase {ECO:0000313|EMBL:SUD48434.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000255467};
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 85..101
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 107..125
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 269..287
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 299..324
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 721..746
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 752..770
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 791..813
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 825..843
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 855..877
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 897..913
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 28..102
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 931 AA; 98014 MW; D9DBF1ED7303822C CRC64;
MRPAERSYDR VVPRAAAEID VPDVVTNAHH GLSAHEVVLL LETDRHRGLS RPEAAKRMAR
FGPNTLPDAP RAGWPMRLLR QLHNPLIYVL LVAGVVTAVL AEYVDSAVIF GVVVINALVG
FVQESKAEAA LEGLRSMVRT QARVVRDGGE RTVPSDELVP GDLVLLDAGD KVPADLRLIQ
VAELRVNESA LTGESAPVAK DEVVLPEGTP VSDRRNMAYS ATLVTAGSGA GIVVATGAET
EVGAIHRLVG AAEDLATPLT RKLSRFSRIL TVGVLVLAAA TFAVGYLRGQ DAAEMFTAAI
ALAVGAIPEG LPAAVTITLA IGVSRMAKRR AVIRQLPAVE TLGSTTVICS DKTGTLTENQ
MTVTTIWTPD GRFEVSGTGY APTGTIGESS GATADSEQHQ ALRWTLLAGA ACNDATLHRD
DGRWTIVGDP TEGALLVAAA KAGLDRERIA RLLPRVATIP FSSHRRYMAT LHRDSGSASA
ADRVALVKGA VEQILDLCPT ALRADGTTTP LDRDAVLTAA DELAARGLRV LATAVRPTAA
PAEFTVDSLA AGLIFTGLQA MLDPARSAVP IAVESCRSAG IAVKMITGDH AATAAAIATR
IGLVDPRDDE SALTGGELDA LPPERFAETV DRTHVFARVS PEQKLRLVEA LQARGHVVAM
TGDGVNDAPA LRQADIGVAM GAGGTEVAKD AADMVLIDDD FATIEAAVEE GRGVFDNLVK
FITWTLPTNI GEGLVLLVAI AAGAALPILP TQILWINMTT AVALGLMLAF EPKEPAIMTR
PPRDPGQPLM TGSLVLRTLL VSTLLVAGTW WLFEWELAHG ASLAEARTAA VNLFVVVEAF
YLFSCRSLTH SAWRIGLFSN PWITGGVALQ AVGQVAITYL PVMNTVFDTA PIAVDSWLRI
AAIAAVASAV VAVDKRLRRP SRSSGTTQSI E
//
