ID   ATCL_MYCPN              Reviewed;         872 AA.
AC   P78036;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=Probable cation-transporting P-type ATPase;
DE            EC=7.2.2.-;
GN   Name=pacL; OrderedLocusNames=MPN_209; ORFNames=MP622;
OS   Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS   pneumoniae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
CC   -!- FUNCTION: Could mediate calcium influx.
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. Type II subfamily. {ECO:0000305}.
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DR   EMBL; U00089; AAB96270.1; -; Genomic_DNA.
DR   PIR; S73948; S73948.
DR   RefSeq; NP_109897.1; NC_000912.1.
DR   RefSeq; WP_010874566.1; NC_000912.1.
DR   AlphaFoldDB; P78036; -.
DR   SMR; P78036; -.
DR   IntAct; P78036; 1.
DR   STRING; 272634.MPN_209; -.
DR   EnsemblBacteria; AAB96270; AAB96270; MPN_209.
DR   KEGG; mpn:MPN_209; -.
DR   PATRIC; fig|272634.6.peg.228; -.
DR   HOGENOM; CLU_002360_1_1_14; -.
DR   OMA; ITFFGWM; -.
DR   BioCyc; MPNE272634:G1GJ3-339-MON; -.
DR   Proteomes; UP000000808; 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; -; 2.
DR   Gene3D; 3.40.50.1000; -; 2.
DR   InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR   InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
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   Pfam; PF00690; Cation_ATPase_N; 1.
DR   PRINTS; PR00120; HATPASE.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SMART; SM00831; Cation_ATPase_N; 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..872
FT                   /note="Probable cation-transporting P-type ATPase"
FT                   /id="PRO_0000046163"
FT   TOPO_DOM        1..41
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        42..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        63..79
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        80..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        101..237
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        238..257
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        258..275
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        276..293
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        294..642
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        643..662
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        663..685
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        686..706
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        707..724
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        725..747
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        748..768
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        769..788
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        789..801
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        802..824
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        825..842
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        843..863
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        864..872
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        331
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         587
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         591
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   872 AA;  94968 MW;  42F8001C4798CAFE CRC64;
     MNKWTGLSAA AVLESRAQHG ANLIPTKKLT PFWLLFLEQF KSLVVILLLV ATILSLVVAI
     ISGVNANWLF DHNLVIEWTQ PFVILITVLA NSLIGSIQEF KAQKSAHTLK SLTQPFTRVF
     REEGLVSLPV GEVVVGDIIF LEAGDIIPAD GKVLQANHLR CMESFLTGES VPVDKSVVNT
     GGKGLLEQTN LLFSGAQVVF GSGVFEVTAV GLNTQVGQIV KTVDSSATKL SPLQQKLEKV
     GKWFSWFGLG LFVVVFLVQL GLLGFHNFSA NWSIALIGAI ALVVAIIPEG LVTFINVIFA
     LSVQKLTKQK AIIKYLAAIE TLGGVQIICT DKTGTLTQNK MKVVDYFCFS NTTQTDLARA
     LCLCNNATVN TNGDSTGDPT EIALLQWLDR DGLELNHYTR VYEKAFDSNR KLMSVVVQKD
     NRFIVIVKGA HDVLLPLCKG LDSNQIKPLI DERASNGLRN LAVGLKVLYC FDPENTQTVN
     ELESELDFLG SVSLQDPPRI ESKAAIMACH QANITPIMIT GDHLKTATAI AKELGILTDE
     RQAILGVDLD PAKIMEYRVF ARVTPQQKLE IVNAWKQAGY TVAVTGDGVN DAPALVTSDV
     GCCMGQTGVD IAKDAADVII SDDNFATIVN GIEQGRKTFL TCKRVLFNLF LTSIAGTIVV
     LLGLFVLGEV FREQLSKANH NFQVFTPTQL LIINLFVHGF PAVALAIQPV QEKLMLKPFS
     TKNLFYNRGG FDLIWQSLLL SFLTLLFYSL GMVYAINDPE LGKSGDLINR AGATCGFMVL
     GGSAALNSLN LMVDRPLVAT NPKHYGIVWL GALSSIFVFL LIIFINPLGL VFSTLKDLTA
     HPVLIGYSFG GVLLYMTINE VVKLIRLSYG SV