CTPF_MYCBO
ID CTPF_MYCBO Reviewed; 905 AA.
AC P63688; A0A1R3Y0A8; Q10860; Q10861; X2BJ82;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Probable cation-transporting ATPase F;
DE EC=7.2.2.-;
GN Name=ctpF; OrderedLocusNames=BQ2027_MB2020;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
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 -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIA subfamily. {ECO:0000305}.
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DR EMBL; LT708304; SIU00627.1; -; Genomic_DNA.
DR RefSeq; NP_855670.1; NC_002945.3.
DR RefSeq; WP_003410027.1; NC_002945.4.
DR AlphaFoldDB; P63688; -.
DR SMR; P63688; -.
DR EnsemblBacteria; SIU00627; SIU00627; BQ2027_MB2020.
DR PATRIC; fig|233413.5.peg.2219; -.
DR OMA; PLWNNMM; -.
DR Proteomes; UP000001419; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:UniProtKB-KW.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 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 Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR PRINTS; PR00120; HATPASE.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 3.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Translocase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..905
FT /note="Probable cation-transporting ATPase F"
FT /id="PRO_0000046342"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 716..736
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 738..758
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 778..798
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 808..828
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 842..862
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 872..892
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 333
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 643
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 647
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 905 AA; 95033 MW; 7A1E6A23CF4D4DA6 CRC64;
MSASVSATTA HHGLPAHEVV LLLESDPYHG LSDGEAAQRL ERFGPNTLAV VTRASLLARI
LRQFHHPLIY VLLVAGTITA GLKEFVDAAV IFGVVVINAI VGFIQESKAE AALQGLRSMV
HTHAKVVREG HEHTMPSEEL VPGDLVLLAA GDKVPADLRL VRQTGLSVNE SALTGESTPV
HKDEVALPEG TPVADRRNIA YSGTLVTAGH GAGIVVATGA ETELGEIHRL VGAAEVVATP
LTAKLAWFSK FLTIAILGLA ALTFGVGLLR RQDAVETFTA AIALAVGAIP EGLPTAVTIT
LAIGMARMAK RRAVIRRLPA VETLGSTTVI CADKTGTLTE NQMTVQSIWT PHGEIRATGT
GYAPDVLLCD TDDAPVPVNA NAALRWSLLA GACSNDAALV RDGTRWQIVG DPTEGAMLVV
AAKAGFNPER LATTLPQVAA IPFSSERQYM ATLHRDGTDH VVLAKGAVER MLDLCGTEMG
ADGALRPLDR ATVLRATEML TSRGLRVLAT GMGAGAGTPD DFDENVIPGS LALTGLQAMS
DPPRAAAASA VAACHSAGIA VKMITGDHAG TATAIATEVG LLDNTEPAAG SVLTGAELAA
LSADQYPEAV DTASVFARVS PEQKLRLVQA LQARGHVVAM TGDGVNDAPA LRQANIGVAM
GRGGTEVAKD AADMVLTDDD FATIEAAVEE GRGVFDNLTK FITWTLPTNL GEGLVILAAI
AVGVALPILP TQILWINMTT AIALGLMLAF EPKEAGIMTR PPRDPDQPLL TGWLVRRTLL
VSTLLVASAW WLFAWELDNG AGLHEARTAA LNLFVVVEAF YLFSCRSLTR SAWRLGMFAN
RWIILGVSAQ AIAQFAITYL PAMNMVFDTA PIDIGVWVRI FAVATAITIV VATDTLLPRI
RAQPP
