ID   CTPI_MYCTU              Reviewed;        1632 AA.
AC   P9WPS5; L0T5J4; Q10900;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=Probable cation-transporting ATPase I;
DE            EC=7.2.2.-;
GN   Name=ctpI; OrderedLocusNames=Rv0107c; ORFNames=MTCY251.26c;
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   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 {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; AL123456; CCP42832.1; -; Genomic_DNA.
DR   PIR; C70752; C70752.
DR   RefSeq; NP_214621.1; NC_000962.3.
DR   RefSeq; WP_010886065.1; NZ_NVQJ01000053.1.
DR   AlphaFoldDB; P9WPS5; -.
DR   SMR; P9WPS5; -.
DR   STRING; 83332.Rv0107c; -.
DR   PaxDb; P9WPS5; -.
DR   PRIDE; P9WPS5; -.
DR   GeneID; 886915; -.
DR   KEGG; mtu:Rv0107c; -.
DR   TubercuList; Rv0107c; -.
DR   eggNOG; COG0474; Bacteria.
DR   PhylomeDB; P9WPS5; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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; 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   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..1632
FT                   /note="Probable cation-transporting ATPase I"
FT                   /id="PRO_0000046347"
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   REGION          1573..1601
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1586..1601
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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   1632 AA;  169607 MW;  A29F651A55EF7FD8 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 SGVPRWDRSP GRASSAPRQE PPQSQRWHRS GWQAQSVSCN LMNALTTRKT
     LTRVDRTYRR PR