CTPC_MYCLE
ID CTPC_MYCLE Reviewed; 725 AA.
AC Q9CCL1;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Manganese-exporting P-type ATPase {ECO:0000250|UniProtKB:P9WPT5};
DE EC=7.2.2.- {ECO:0000250|UniProtKB:P9WPT5};
GN Name=ctpC; OrderedLocusNames=ML0747;
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 -!- FUNCTION: High affinity, slow turnover Mn(2+) transporting ATPase.
CC {ECO:0000250|UniProtKB:P9WPT5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + Mn(2+)(in) = ADP + H(+) + Mn(2+)(out) + phosphate;
CC Xref=Rhea:RHEA:66820, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29035, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P9WPT5};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P9WPT5};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P9WPT5}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IB subfamily. {ECO:0000305}.
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DR EMBL; AL583919; CAC30256.1; -; Genomic_DNA.
DR PIR; D87002; D87002.
DR RefSeq; NP_301578.1; NC_002677.1.
DR RefSeq; WP_010907902.1; NC_002677.1.
DR AlphaFoldDB; Q9CCL1; -.
DR SMR; Q9CCL1; -.
DR STRING; 272631.ML0747; -.
DR EnsemblBacteria; CAC30256; CAC30256; CAC30256.
DR KEGG; mle:ML0747; -.
DR PATRIC; fig|272631.5.peg.1356; -.
DR Leproma; ML0747; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_6_4_11; -.
DR OMA; IVTWLFM; -.
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 GO; GO:0140613; F:P-type manganese transporter activity; IEA:RHEA.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
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; IPR027256; P-typ_ATPase_IB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01525; ATPase-IB_hvy; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS50846; HMA_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Magnesium; Manganese; Membrane; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Translocase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..725
FT /note="Manganese-exporting P-type ATPase"
FT /id="PRO_0000046336"
FT TRANSMEM 101..119
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P9WPT5"
FT TRANSMEM 142..160
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P9WPT5"
FT TRANSMEM 165..179
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P9WPT5"
FT TRANSMEM 188..202
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P9WPT5"
FT TRANSMEM 335..359
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P9WPT5"
FT TRANSMEM 365..383
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P9WPT5"
FT TRANSMEM 669..688
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P9WPT5"
FT TRANSMEM 698..717
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P9WPT5"
FT DOMAIN 25..92
FT /note="HMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT ACT_SITE 416
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q5ZWR1"
FT BINDING 416
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q5ZWR1"
FT BINDING 418
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q5ZWR1"
FT BINDING 618
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q5ZWR1"
SQ SEQUENCE 725 AA; 77156 MW; 7B134A664ED7462B CRC64;
MTLAMAEQIA TADNPAFVVV SDAAGRMRIQ IEWVRSNPRR AVTVEEAIAK CNGVRVVHAY
PRTGSVVVWY SPRCCDRQSI LAAISGAAHV AAELIPTRAP HSSDIRNIEV LRMAIGAAAL
TLLGVRRYVF ARPLLLPTTS RLVASGVTIF TGYPFLRGAL RFGKTGTDAL VSVATIASLI
LRENVVALAV LWLLNIGEYL QDLTLRRTRR AISALLSGTQ DTAWIRLTDG PQAGTEIQVP
IGTVQIGDEV VVHEHVAIPV DGEVIDGEAV VNQSAITGEN LPVSVMAGSH VHAGSVVVRG
RLMVRASAVG KHTTIGRIVT RVEEAQHDRA PIQTVGENFS RCFVPTSFVV SAITLAITKD
VRRTMTVLLI ACPCAVGLAT PTAISAAIGN GARRGILIKG GSHLEQAGRV DAILFDKTGT
LTVGRPVVTN IVAMHKDWSP EQVLAYAASS EIHSRHPLAE AVIRSTEERH ISIPPHEECE
VLVGLGMRTW ADGRTLLLGS PSLLCAEKVK VSKTASEWVD KLRHQTETPL LFAVDGTLVG
LISLRDEVRP EAAEVLTKLR ASGVRRIVML TGDHPDIAKA VATELGIDEW RAEVMPEDKL
KVVRDLQNEG YVVGMVGDGV NDAPALAAAD IGIAMGLAGT DVAVETADVA LANDDLNRLL
DVRDLGGRAV EVIRENYGMS IAVNAAGLFI GAGGALSPVL AAVLHNASSV AVVANSSRLI
RYRLD
