CTPF_MYCTO
ID CTPF_MYCTO Reviewed; 905 AA.
AC P9WPS8; 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 44.
DE RecName: Full=Probable cation-transporting ATPase F;
DE EC=7.2.2.-;
GN Name=ctpF; OrderedLocusNames=MT2053;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
RN [2]
RP INDUCTION BY NITRIC OXIDE (NO) AND BY HYPOXIA, AND DORMANCY REGULON.
RC STRAIN=CDC 1551 / Oshkosh;
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).
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 {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: A member of the dormancy regulon. Induced in response to
CC reduced oxygen tension (hypoxia) and low levels of nitric oxide (NO).
CC {ECO:0000269|PubMed:12953092}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIA subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK46330.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE000516; AAK46330.1; ALT_INIT; Genomic_DNA.
DR PIR; C70758; C70758.
DR RefSeq; WP_003410027.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WPS8; -.
DR SMR; P9WPS8; -.
DR EnsemblBacteria; AAK46330; AAK46330; MT2053.
DR KEGG; mtc:MT2053; -.
DR PATRIC; fig|83331.31.peg.2210; -.
DR HOGENOM; CLU_002360_3_3_11; -.
DR Proteomes; UP000001020; 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 2: Evidence at transcript level;
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_0000426894"
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
