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EXP7_STRPN
ID   EXP7_STRPN              Reviewed;         778 AA.
AC   P35597;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   26-SEP-2001, sequence version 2.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Probable cation-transporting ATPase exp7;
DE            EC=7.2.2.-;
DE   AltName: Full=Exported protein 7;
GN   Name=exp7; OrderedLocusNames=SP_1623;
OS   Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=170187;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-334 / TIGR4;
RX   PubMed=11463916; DOI=10.1126/science.1061217;
RA   Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA   Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA   Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA   Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA   Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA   McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA   Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA   Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT   "Complete genome sequence of a virulent isolate of Streptococcus
RT   pneumoniae.";
RL   Science 293:498-506(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 402-482.
RC   STRAIN=R6x;
RX   PubMed=7934910; DOI=10.1111/j.1365-2958.1993.tb01233.x;
RA   Pearce B.J., Yin Y.B., Masure H.R.;
RT   "Genetic identification of exported proteins in Streptococcus pneumoniae.";
RL   Mol. Microbiol. 9:1037-1050(1993).
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 {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. {ECO:0000305}.
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DR   EMBL; AE005672; AAK75703.1; -; Genomic_DNA.
DR   EMBL; L20561; AAA26883.1; -; Genomic_DNA.
DR   PIR; F95188; F95188.
DR   RefSeq; WP_000360054.1; NZ_AKVY01000001.1.
DR   AlphaFoldDB; P35597; -.
DR   SMR; P35597; -.
DR   STRING; 170187.SP_1623; -.
DR   DNASU; 931480; -.
DR   EnsemblBacteria; AAK75703; AAK75703; SP_1623.
DR   KEGG; spn:SP_1623; -.
DR   eggNOG; COG0474; Bacteria.
DR   OMA; FFIKTIY; -.
DR   PhylomeDB; P35597; -.
DR   BioCyc; SPNE170187:G1FZB-1642-MON; -.
DR   Proteomes; UP000000585; 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; -; 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; 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; SSF81660; SSF81660; 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; Translocase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..778
FT                   /note="Probable cation-transporting ATPase exp7"
FT                   /id="PRO_0000046186"
FT   TOPO_DOM        1..37
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        38..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        58..64
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        65..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        85..209
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        210..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        230..242
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        243..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        261..586
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        587..606
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        607..624
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        625..645
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        646..663
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        664..684
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        685..689
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        690..708
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        709..716
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        717..739
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        740..757
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        758..777
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        778
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        298
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         532
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         536
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        402..411
FT                   /note="ERGSRVLVLA -> TASEFELGTP (in Ref. 2; AAA26883)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   778 AA;  85531 MW;  1154C1FAF9DF7818 CRC64;
     MDKNKIMGLT QREVKERQAE GLVNDFTASA STSTWQIVKR NVFTLFNALN FAIALALAFV
     QAWSNLVFFA VICFNAFSGI VTELRAKHMV DKLNLMTKEK VKTIRDGQEV ALNPEELVLG
     DVIRLSAGEQ IPSDALVLEG FAEVNEAMLT GESDLVQKEV DGLLLSGSFL ASGSVLSQVH
     HVGADNYAAK LMLEAKTVKP INSRIMKSLD KLAGFTGKII IPFGLALLLE ALLLKGLPLK
     SSVVNSSTAL LGMLPKGIAL LTITSLLTAV IKLGLKKVLV QEMYSVETLA RVDMLCLDKT
     GTITQGKMQV EAVLPLTETY GEEAIASILT SYMAHSEDKN PTAQAIRQRF VGDVAYPMIS
     NLPFSSDRKW GAMELEGLGT VFLGAPEMLL DSEVPEAREA LERGSRVLVL ALSQEKLDHH
     KPQKPSDIQA LALLEILDPI REGAAETLDY LRSQEVGLKI ISGDNPVTVS SIAQKAGFAD
     YHSYVDCSKI TDEELMAMAE ETAIFGRVSP HQKKLIIQTL KKAGHTTAMT GDGVNDILAL
     READCSIVMA EGDPATRQIA NLVLLNSDFN DVPEILFEGR RVVNNIAHIA PIFLIKTIYS
     FLLAVICIAS ALLGRSEWIL IFPFIPIQIT MIDQFVEGFP PFVLTFERNI KPVEQNFLRK
     SMLRALPSAL MVVFSVLFVK MFGASQGWSE LEISTLLYYL LGSIGFLSVF RACMPFTLWR
     VLLIVWSVGG FLATALFPRI QKLLEISTLT EQTLPVYGVM MLVFTVIFIL TSRYQAKK
 
 
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