CTPC_MYCMM
ID CTPC_MYCMM Reviewed; 732 AA.
AC B2HEM2;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Zinc-exporting P-type ATPase {ECO:0000305};
DE EC=7.2.2.12 {ECO:0000305|PubMed:33531393};
DE AltName: Full=Zn(2+) efflux pump CtpC {ECO:0000303|PubMed:33531393};
GN Name=ctpC {ECO:0000303|PubMed:33531393};
GN OrderedLocusNames=MMAR_1271 {ECO:0000312|EMBL:ACC39729.1};
OS Mycobacterium marinum (strain ATCC BAA-535 / M).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=216594;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-535 / M;
RX PubMed=18403782; DOI=10.1101/gr.075069.107;
RA Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT "Insights from the complete genome sequence of Mycobacterium marinum on the
RT evolution of Mycobacterium tuberculosis.";
RL Genome Res. 18:729-741(2008).
RN [2]
RP FUNCTION AS A ZINC EXPORTER, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-535 / M;
RX PubMed=33531393; DOI=10.1128/mbio.01313-20;
RA Hanna N., Koliwer-Brandl H., Lefrancois L.H., Kalinina V.,
RA Cardenal-Munoz E., Appiah J., Leuba F., Gueho A., Hilbi H., Soldati T.,
RA Barisch C.;
RT "Zn2+ intoxication of Mycobacterium marinum during Dictyostelium discoideum
RT infection is counteracted by induction of the pathogen Zn2+ exporter
RT CtpC.";
RL MBio 12:e01313-e01313(2021).
CC -!- FUNCTION: Zn(2+) efflux transporter which is involved in detoxification
CC of zinc during infection. {ECO:0000269|PubMed:33531393}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + Zn(2+)(in) = ADP + H(+) + phosphate + Zn(2+)(out);
CC Xref=Rhea:RHEA:20621, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29105, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; EC=7.2.2.12;
CC Evidence={ECO:0000305|PubMed:33531393};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20622;
CC Evidence={ECO:0000305|PubMed:33531393};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Induced during infection of D.discoideum and by elevated
CC levels of Zn(2+). {ECO:0000269|PubMed:33531393}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene leads to growth inhibition
CC in the presence of elevated levels of Zn(2+), but not Mn(2+) or Cu(2+)
CC (PubMed:33531393). Deletion mutant shows strongly attenuated
CC intracellular growth during D.discoideum infection (PubMed:33531393).
CC {ECO:0000269|PubMed:33531393}.
CC -!- MISCELLANEOUS: Increasing concentrations of Mn(2+) does not affect the
CC growth of the wild-type strain, nor that of the deletion mutant,
CC excluding that M.marinum CtpC is a manganese exporter as M.tuberculosis
CC CtpC. {ECO:0000269|PubMed:33531393}.
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; CP000854; ACC39729.1; -; Genomic_DNA.
DR RefSeq; WP_012393144.1; NC_010612.1.
DR STRING; 216594.MMAR_1271; -.
DR EnsemblBacteria; ACC39729; ACC39729; MMAR_1271.
DR KEGG; mmi:MMAR_1271; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_6_3_11; -.
DR OMA; IVTWLFM; -.
DR OrthoDB; 237367at2; -.
DR Proteomes; UP000001190; 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-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled cation transmembrane transporter 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; 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 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Ion transport; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Reference proteome; Translocase;
KW Transmembrane; Transmembrane helix; Transport; Virulence; Zinc;
KW Zinc transport.
FT CHAIN 1..732
FT /note="Zinc-exporting P-type ATPase"
FT /id="PRO_0000455994"
FT TRANSMEM 105..123
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P9WPT5"
FT TRANSMEM 146..164
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P9WPT5"
FT TRANSMEM 172..186
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P9WPT5"
FT TRANSMEM 195..209
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P9WPT5"
FT TRANSMEM 342..366
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P9WPT5"
FT TRANSMEM 372..390
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P9WPT5"
FT TRANSMEM 676..695
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P9WPT5"
FT TRANSMEM 705..724
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P9WPT5"
FT DOMAIN 29..96
FT /note="HMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT ACT_SITE 423
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q5ZWR1"
FT BINDING 423
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q5ZWR1"
FT BINDING 425
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q5ZWR1"
FT BINDING 625
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q5ZWR1"
SQ SEQUENCE 732 AA; 77846 MW; DF612F0A6ADF1878 CRC64;
MTLAIVKEVP AGADGDDTTD LVVLSDAAGR MRVRADWVRG NSRRAVAVEE AVAKQDGVRV
VHAYPRTGSV VVWYSPRRCD RAAVLEAIGG AKHVAAELIP ARAPHSTEIR NTDVLRMVIG
GAALALLGVR RYVFARPPLL GPSGRMVATG VTIFTGYPFL RGALRSLRSG KAGTDALVSA
ATIASLILRE NVVALTVLWL LNIGEYLQDL TLRRTRRAIS ELLRGNQDTA WIRLTDGPEA
GTEVQVPIDS VQIGDEVVVH DHVAIPVDGE VVDGEAIVNQ SAITGENLPV SVVAGATVHA
GSVVVRGRLV VRAQAVGNQT TIGRIITRVE EAQNDRAPIQ TVGENFSRRF VPTSFIVSAI
TLLVTGDVRR AMTMLLIACP CAVGLSTPTA ISAAIGNGAR RGILIKGGSH LEQAGRVDAI
VFDKTGTLTV GRPVVTNIIA MHKDWEPEQV LAYAASSEIH SRHPLAEAVI RSTEERRISI
PPHEECEVLV GLGMRTWADG RTLLLGSPSL LESEQVKVSK KASEWVGKLR QQAETPLLLA
VDGTLVGLIS LRDEVRPEAA EVLTKLRDNG VRRIVMLTGD HPDIAKVVAE ELGIDEWRAE
VMPEDKLEVV RDLQDEGYVV GMVGDGINDA PALAAADIGI AMGLAGTDVA VETADVALAN
DDLHRLLDVR DLGGRAVDVI RQNYGMSIAV NAAGLLIGAG GALSPVLAAI LHNASSVAVV
ANSSRLIRYR LE
