CTPF_MYCTU
ID CTPF_MYCTU Reviewed; 905 AA.
AC P9WPS9; L0TB76; P63687; Q10860; Q10861;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Probable cation-transporting ATPase F;
DE EC=7.2.2.-;
GN Name=ctpF; OrderedLocusNames=Rv1997; ORFNames=MTCY39.21c, MTCY39.22c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP INDUCTION BY HYPOXIA.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=11416222; DOI=10.1073/pnas.121172498;
RA Sherman D.R., Voskuil M., Schnappinger D., Liao R., Harrell M.I.,
RA Schoolnik G.K.;
RT "Regulation of the Mycobacterium tuberculosis hypoxic response gene
RT encoding alpha -crystallin.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7534-7539(2001).
RN [3]
RP INDUCTION BY NITRIC OXIDE (NO) AND BY HYPOXIA, AND DORMANCY REGULON.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=12953092; DOI=10.1084/jem.20030205;
RA Voskuil M.I., Schnappinger D., Visconti K.C., Harrell M.I., Dolganov G.M.,
RA Sherman D.R., Schoolnik G.K.;
RT "Inhibition of respiration by nitric oxide induces a Mycobacterium
RT tuberculosis dormancy program.";
RL J. Exp. Med. 198:705-713(2003).
RN [4]
RP INDUCTION BY CARBON MONOXIDE (CO).
RC STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX PubMed=18474359; DOI=10.1016/j.chom.2008.03.007;
RA Shiloh M.U., Manzanillo P., Cox J.S.;
RT "Mycobacterium tuberculosis senses host-derived carbon monoxide during
RT macrophage infection.";
RL Cell Host Microbe 3:323-330(2008).
RN [5]
RP INDUCTION BY CARBON MONOXIDE (CO), AND DORMANCY REGULON.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=18400743; DOI=10.1074/jbc.m802274200;
RA Kumar A., Deshane J.S., Crossman D.K., Bolisetty S., Yan B.S., Kramnik I.,
RA Agarwal A., Steyn A.J.;
RT "Heme oxygenase-1-derived carbon monoxide induces the Mycobacterium
RT tuberculosis dormancy regulon.";
RL J. Biol. Chem. 283:18032-18039(2008).
RN [6]
RP BIOTECHNOLOGY.
RX PubMed=19553548; DOI=10.1128/cvi.00111-09;
RA Black G.F., Thiel B.A., Ota M.O., Parida S.K., Adegbola R., Boom W.H.,
RA Dockrell H.M., Franken K.L., Friggen A.H., Hill P.C., Klein M.R.,
RA Lalor M.K., Mayanja H., Schoolnik G., Stanley K., Weldingh K.,
RA Kaufmann S.H., Walzl G., Ottenhoff T.H.;
RT "Immunogenicity of novel DosR regulon-encoded candidate antigens of
RT Mycobacterium tuberculosis in three high-burden populations in Africa.";
RL Clin. Vaccine Immunol. 16:1203-1212(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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 -!- INDUCTION: A member of the dormancy regulon. Induced in response to
CC reduced oxygen tension (hypoxia), low levels of nitric oxide (NO) and
CC carbon monoxide (CO). It is hoped that this regulon will give insight
CC into the latent, or dormant phase of infection.
CC {ECO:0000269|PubMed:11416222, ECO:0000269|PubMed:12953092,
CC ECO:0000269|PubMed:18400743, ECO:0000269|PubMed:18474359}.
CC -!- BIOTECHNOLOGY: This protein serves as an immunogenic antigen, inducing
CC gamma-interferon responses in whole-blood cultures from M.tuberculosis-
CC exposed adults in Uganda and South Africa, indicating this might be a
CC good vaccine candidate. {ECO:0000269|PubMed:19553548}.
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; AL123456; CCP44769.1; -; Genomic_DNA.
DR PIR; C70758; C70758.
DR RefSeq; NP_216513.1; NC_000962.3.
DR RefSeq; WP_003410027.1; NZ_NVQJ01000043.1.
DR AlphaFoldDB; P9WPS9; -.
DR SMR; P9WPS9; -.
DR STRING; 83332.Rv1997; -.
DR PaxDb; P9WPS9; -.
DR GeneID; 888867; -.
DR KEGG; mtu:Rv1997; -.
DR TubercuList; Rv1997; -.
DR eggNOG; COG0474; Bacteria.
DR OMA; PLWNNMM; -.
DR PhylomeDB; P9WPS9; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; HDA:MTBBASE.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled cation transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005388; F:P-type calcium transporter activity; IBA:GO_Central.
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 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..905
FT /note="Probable cation-transporting ATPase F"
FT /id="PRO_0000046343"
FT TRANSMEM 64..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..301
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
