CTPI_MYCTO
ID CTPI_MYCTO Reviewed; 1625 AA.
AC P9WPS4; L0T5J4; Q10900;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Probable cation-transporting ATPase I;
DE EC=7.2.2.-;
GN Name=ctpI; OrderedLocusNames=MT0116;
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).
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 -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. {ECO:0000305}.
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DR EMBL; AE000516; AAK44338.1; -; Genomic_DNA.
DR PIR; C70752; C70752.
DR RefSeq; WP_003899815.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WPS4; -.
DR SMR; P9WPS4; -.
DR EnsemblBacteria; AAK44338; AAK44338; MT0116.
DR KEGG; mtc:MT0116; -.
DR PATRIC; fig|83331.31.peg.121; -.
DR HOGENOM; CLU_002360_0_1_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; 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 PRINTS; PR00120; HATPASE.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 2.
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..1625
FT /note="Probable cation-transporting ATPase I"
FT /id="PRO_0000426896"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 358..378
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 637..657
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 673..693
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 778..798
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 968..988
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 997..1017
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1401..1421
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1432..1452
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1547..1567
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 1053
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 1340
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1344
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1625 AA; 167806 MW; 54082AD7064C22EB CRC64;
MKIPGVATVL GGVTNGVAQT VRAGARLPGS AAAAVQTLAS PVLELTGPVV QSVVQTTGRA
IGVRGSHNES PDGMTPPVRW RSGRRVHFDL DPLLPFPRWH EHAAMVEEPV RRIPGVAEAH
VEGSLGRLVV ELEPDADSDI AVDEVRDVVS AVAADIFLAG SVSSPNSAPF ADPGNPLAIL
VPLTAAAMDL VAMGATVTGW VARLPAAPQT TRALAALINH QPRMVSLMES RLGRVGTDIA
LAATTAAANG LTQSLGTPLL DLVQRSLQIS EAAAHRRVWR DREPALASPR RPQAPVVPII
SSAGAKSQEP RHSWAAAAAG EASHVVVGGS IDAAIDTAKG SRAGPVEQYV NQAANGSLIA
AASALVAGGG TEDAAGAILA GVPRAAHMGR QAFAAVLGRG LANTGQLVLD PGALRRLDRV
RVVVIDGAAL RGDNRAVLHA QGDEPGWDDD RVYEVADALL HGEQAPEPDP DELPATGARL
RWAPAQGPSA TPAQGLEHAD LVVDGQCVGS VDVGWEVDPY AIPLLQTAHR TGARVVLRHV
AGTEDLSASV GSTHPPGTPL LKLVRELRAD RGPVLLITAV HRDFASTDTL AALAIADVGV
ALDDPRGATP WTADLITGTD LAAAVRILSA LPVARAASES AVHLAQGGTT LAGLLLVTGE
QDKTTNPASF RRWLNPVNAA AATALVSGMW SAAKVLRMPD PTPQPLTAWH ALDPEIVYSR
LAGGSRPLAV EPGIPAWRRI LDDLSYEPVM APLRGPARTL AQLAVATRHE LADPLTPILA
VGAAASAIVG SNIDALLVAG VMTVNAITGG VQRLRAEAAA AELFAEQDQL VRRVVVPAVA
TTRRRLEAAR HATRTATVSA KSLRVGDVID LAAPEVVPAD ARLLVAEDLE VDESFLTGES
LPVDKQVDPV AVNDPDRASM LFEGSTIVAG HARAIVVATG VGTAAHRAIS AVADVETAAG
VQARLRELTS KVLPMTLAGG AAVTALALLR RASLRQAVAD GVAIAVAAVP EGLPLVATLS
QLAAAQRLTA RGALVRSPRT IEALGRVDTI CFDKTGTLTE NRLRVVCALP SSTAAERDPL
PQTTDAPSAE VLRAAARAST QPHNGEGHAH ATDEAILAAA SALAGSLSSQ GDSEWVVLAE
VPFESSRGYA AAIGRVGTDG IPMLMLKGAP ETILPRCRLA DPGVDHEHAE SVVRHLAEQG
LRVLAVAQRT WDNGTTHDDE TDADAVDAVA HDLELIGYVG LADTARSSSR PLIEALLDAE
RNVVLITGDH PITARAIARQ LGLPADARVV TGAELAVLDE EAHAKLAADM QVFARVSPEQ
KVQIVAALQR CGRVTAMVGD GANDAAAIRM ADVGIGVSGR GSSAARGAAD IVLTDDDLGV
LLDALVEGRS MWAGVRDAVT ILVGGNVGEV LFTVIGTAFG AGRAPVGTRQ LLLVNLLTDM
FPALAVAVTS QFAEPDDAEY PTDDAAERAQ REHRRAVLIG PTPSLDAPLL RQIVNRGVVT
AAGATAAWAI GRWTPGTERR TATMGLTALV MTQLAQTLLT RRHSPLVIAT ALGSAGVLVG
IIQTPVISHF FGCTPLGPVA WTGVFSATAG ATAVSALAPK WLASTVGVVQ PDERPDDAED
SDAGG