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CTPI_MYCLE
ID   CTPI_MYCLE              Reviewed;        1609 AA.
AC   O53114;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Probable cation-transporting ATPase I;
DE            EC=7.2.2.-;
GN   Name=ctpI; OrderedLocusNames=ML2671; ORFNames=MLCB1913.02;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
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. {ECO:0000305}.
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DR   EMBL; AL022118; CAA17934.1; -; Genomic_DNA.
DR   EMBL; AL583926; CAC32203.1; -; Genomic_DNA.
DR   PIR; E87243; E87243.
DR   RefSeq; NP_302704.1; NC_002677.1.
DR   AlphaFoldDB; O53114; -.
DR   SMR; O53114; -.
DR   STRING; 272631.ML2671; -.
DR   EnsemblBacteria; CAC32203; CAC32203; CAC32203.
DR   KEGG; mle:ML2671; -.
DR   PATRIC; fig|272631.5.peg.5145; -.
DR   Leproma; ML2671; -.
DR   eggNOG; COG0474; Bacteria.
DR   HOGENOM; CLU_002360_0_1_11; -.
DR   OMA; PKAARYG; -.
DR   Proteomes; UP000000806; 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; -; 2.
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; Reference proteome; Translocase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..1609
FT                   /note="Probable cation-transporting ATPase I"
FT                   /id="PRO_0000046346"
FT   TRANSMEM        30..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        176..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        238..258
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        357..377
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        641..661
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        921..941
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        969..989
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        997..1017
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1396..1416
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1426..1446
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1542..1562
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1573..1593
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1447..1476
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1053
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         1335
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         1339
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1609 AA;  166873 MW;  58FA2079905E3995 CRC64;
     MKIPHVTDPV SNMVGGMAQV VRASTHAATG AVNTMQMLAS PVAEFAWPVV QSVAKSTGRA
     LGTGHSPNFA NRVDPPVRWH NGQRVHLDLD PLLPFPRWHE YAAVVEEPVR RIPGVAKGHV
     EGSLGRLVIE LDKNADSDVV LGKVRDVVIA LAADLALTGA RSAPKVAPFA DPGNPLAILM
     PLTAAVMDLV ALSAAVTGWV TRLPAVPQTI RAAAALVNHQ PRMVSLLESR LGRVGTDIAL
     SITTAAASGL TQAVGTPLLD LACRGLQLSE AAAHQRVWRD REPQLASPKR PQAPVVPVIS
     SAGEKSHAAG HNWTAAASNE ASHLVVGGSI DAAIDTAKGS MKGPVESYVD SAANGSLIAA
     ASALLAGGGT EDAAGAILAG VPRAAHMGQQ AFAATLGRGL ANAGQLVLDP GALRRLDQVK
     VVVIDGAALR GDHRAVLLAR GNTPGWDDDR VYEVTDALLH GERAPEPDPD ESPATGARLR
     WVPLQGPSAT PVQGREHADL VVNGECVGGV DVGWEVDPYA IPLLQTAHRT GARVVLRHVA
     GTEDLSASVG ATHPPGTPLL KLVRELRTDR GPVLLITAVH RDFASTDTLA ALAIADVGVA
     LDDPHAATPW TADIITGTDL AAAVRILSAL PVARSASESS VHLAQGGTTL AGLLLITASA
     GSKSASPITL RRWFSPVNAA AATALVTGVV SASKVLRLPD PTPQPLTAWH ALDPEIVYSR
     LAGVTQPLAV EPGTPDWRRR LDDLSYTRAL SPLRKPVTKL ARLASATRQE FADPLTPILA
     VGAAASAIVG SNIDALLVAG VMTVNAITGG VQRLRAEAAA AELFAEQDQL VRRVVVPAVA
     TTRRRLEAAQ HATRTVTVSA KSLRAGDVID LAAPEVVPAD ARVLVAEDLE VDESLLTGES
     LPVDKRVDPV AINDADRASM LFEGSAIVAG HARAIVVATG VGTAAHRAIS AVADVEVSAG
     VQARLRELTS KVLPLTLAGG AAVTGLALLR RASLRQAVAD GVAIAVAAVP EGLPLVATLS
     QLAAAQRLTA KGALVRSPRT IEALGRVDTI CFDKTGTLTE NRLRVVCAVP NTRMPHDPLP
     DITDPHSAAV LRDAARASTQ PHDGQGHTHA TDEAILTAAS SLNSHTDSTW SLIAEVPFES
     SRGYAAAIGI TGNGKAPMLM LKGAPEKILP RCRFADPEAD VAHAESLVRH LAEQGLRVLA
     VAQCSWGHDT TDDNDTDADA VDAAAHDLEL VGYIGLADTA RPSSRPLIEA LVTAGRNVVL
     ITGDHPITAR AIAQQLGLRS DARVVNGTEL IGLDEDACAE LAADVQVFAR VSPEQKVQIV
     AALQRCGQVT AMVGDGANDA AAIRMADVGI GVSGRGSSAA RGAADIVLTD DDLGVLLDAL
     VEGRSMWAGV RDAVTILVGG NVGEVVFTII GTVFGAGRAP VGTRQLLLVN LLTDMFPALS
     IAVTSQYEEP GEDEYQTDEE ADEARRTHQH EVLTGPTPSL DAPLMRQIVN RGVVTAAGAT
     TAWAIGRWTP GTERRTATMG LTALVTTQLA QTLLTRRHSP LVVATALGSA GVLIGIIQTP
     VISQFFGCTP LGPIAWSGVI TATAGATAVS VLAPQWLNKA FGIAQLNQE
 
 
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