ID   CTPC_MYCBO              Reviewed;         718 AA.
AC   P0A503; A0A1R3Y3T1; O66027; P96875; X2BNH2;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Manganese-exporting P-type ATPase {ECO:0000250|UniProtKB:P9WPT5};
DE            EC=7.2.2.- {ECO:0000250|UniProtKB:P9WPT5};
GN   Name=ctpC; Synonyms=mtaA; OrderedLocusNames=BQ2027_MB3298;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LT708304; SIU01927.1; -; Genomic_DNA.
DR   RefSeq; NP_856943.1; NC_002945.3.
DR   RefSeq; WP_003899995.1; NC_002945.4.
DR   AlphaFoldDB; P0A503; -.
DR   SMR; P0A503; -.
DR   TCDB; 3.A.3.32.2; the p-type atpase (p-atpase) superfamily.
DR   EnsemblBacteria; SIU01927; SIU01927; BQ2027_MB3298.
DR   PATRIC; fig|233413.5.peg.3627; -.
DR   OMA; IVTWLFM; -.
DR   Proteomes; UP000001419; 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; Translocase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..718
FT                   /note="Manganese-exporting P-type ATPase"
FT                   /id="PRO_0000046335"
FT   TRANSMEM        87..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P9WPT5"
FT   TRANSMEM        128..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P9WPT5"
FT   TRANSMEM        154..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P9WPT5"
FT   TRANSMEM        177..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P9WPT5"
FT   TRANSMEM        327..351
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P9WPT5"
FT   TRANSMEM        357..375
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P9WPT5"
FT   TRANSMEM        661..680
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P9WPT5"
FT   TRANSMEM        690..709
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P9WPT5"
FT   DOMAIN          11..78
FT                   /note="HMA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   ACT_SITE        408
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:Q5ZWR1"
FT   BINDING         408
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q5ZWR1"
FT   BINDING         410
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q5ZWR1"
FT   BINDING         610
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q5ZWR1"
SQ   SEQUENCE   718 AA;  76495 MW;  85D6C93AFE636315 CRC64;
     MTLEVVSDAA GRMRVKVDWV RCDSRRAVAV EEAVAKQNGV RVVHAYPRTG SVVVWYSPRR
     ADRAAVLAAI KGAAHVAAEL IPARAPHSAE IRNTDVLRMV IGGVALALLG VRRYVFARPP
     LLGTTGRTVA TGVTIFTGYP FLRGALRSLR SGKAGTDALV SAATVASLIL RENVVALTVL
     WLLNIGEYLQ DLTLRRTRRA ISELLRGNQD TAWVRLTDPS AGSDAATEIQ VPIDTVQIGD
     EVVVHEHVAI PVDGEVVDGE AIVNQSAITG ENLPVSVVVG TRVHAGSVVV RGRVVVRAHA
     VGNQTTIGRI ISRVEEAQLD RAPIQTVGEN FSRRFVPTSF IVSAIALLIT GDVRRAMTML
     LIACPCAVGL STPTAISAAI GNGARRGILI KGGSHLEQAG RVDAIVFDKT GTLTVGRPVV
     TNIVAMHKDW EPEQVLAYAA SSEIHSRHPL AEAVIRSTEE RRISIPPHEE CEVLVGLGMR
     TWADGRTLLL GSPSLLRAEK VRVSKKASEW VDKLRRQAET PLLLAVDGTL VGLISLRDEV
     RPEAAQVLTK LRANGIRRIV MLTGDHPEIA QVVADELGID EWRAEVMPED KLAAVRELQD
     DGYVVGMVGD GINDAPALAA ADIGIAMGLA GTDVAVETAD VALANDDLHR LLDVGDLGER
     AVDVIRQNYG MSIAVNAAGL LIGAGGALSP VLAAILHNAS SVAVVANSSR LIRYRLDR