ID   BPPI_STRP6              Reviewed;         470 AA.
AC   Q5XAQ1;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Putative bifunctional phosphatase/peptidyl-prolyl cis-trans isomerase;
DE   Includes:
DE     RecName: Full=Phosphatase;
DE              EC=3.1.3.-;
DE   Includes:
DE     RecName: Full=Peptidyl-prolyl cis-trans isomerase;
DE              Short=PPIase;
DE              EC=5.2.1.8;
DE     AltName: Full=Rotamase;
GN   OrderedLocusNames=M6_Spy1377;
OS   Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=286636;
RN   [1] {ECO:0000312|EMBL:AAT87512.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-946 / MGAS10394;
RX   PubMed=15272401; DOI=10.1086/422697;
RA   Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E.,
RA   Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M.;
RT   "Progress toward characterization of the group A Streptococcus metagenome:
RT   complete genome sequence of a macrolide-resistant serotype M6 strain.";
RL   J. Infect. Dis. 190:727-738(2004).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 294-331; 371-394 AND 428-458, AND MASS SPECTROMETRY.
RC   STRAIN=JRS4 / Serotype M6 {ECO:0000269|Ref.2};
RA   Hogan D.A., Du P., Stevenson T.I., Whitton M., Kilby G.W., Rogers J.,
RA   VanBogelen R.A.;
RT   "Two-dimensional gel electrophoresis map of Streptococcus pyogenes
RT   proteins.";
RL   Submitted (MAY-2000) to UniProtKB.
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC       cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides (By similarity). {ECO:0000250|UniProtKB:Q9H2H8}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC         peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC         COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC         ChEBI:CHEBI:83834; EC=5.2.1.8;
CC         Evidence={ECO:0000250|UniProtKB:Q9H2H8};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P0A8Y5};
CC   -!- MASS SPECTROMETRY: Mass=52146.29; Method=Electrospray;
CC       Evidence={ECO:0000269|Ref.2};
CC   -!- SIMILARITY: In the N-terminal section; belongs to the HAD-like
CC       hydrolase superfamily. Cof family. {ECO:0000255}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the cyclophilin-type
CC       PPIase family. PPIL1 subfamily. {ECO:0000255}.
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DR   EMBL; CP000003; AAT87512.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5XAQ1; -.
DR   SMR; Q5XAQ1; -.
DR   EnsemblBacteria; AAT87512; AAT87512; M6_Spy1377.
DR   KEGG; spa:M6_Spy1377; -.
DR   HOGENOM; CLU_046853_0_0_9; -.
DR   OMA; HKGPKAT; -.
DR   Proteomes; UP000001167; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016791; F:phosphatase activity; IEA:UniProt.
DR   GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
DR   Gene3D; 2.40.100.10; -; 1.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR000150; Cof.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   InterPro; IPR044666; Cyclophilin_A-like.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006379; HAD-SF_hydro_IIB.
DR   InterPro; IPR023214; HAD_sf.
DR   PANTHER; PTHR45625; PTHR45625; 2.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SUPFAM; SSF50891; SSF50891; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR00099; Cof-subfamily; 1.
DR   TIGRFAMs; TIGR01484; HAD-SF-IIB; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Isomerase; Magnesium; Metal-binding;
KW   Rotamase.
FT   CHAIN           1..470
FT                   /note="Putative bifunctional phosphatase/peptidyl-prolyl
FT                   cis-trans isomerase"
FT                   /id="PRO_0000308515"
FT   DOMAIN          286..468
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   ACT_SITE        22
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P0A8Y5"
FT   BINDING         22
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P0A8Y5"
FT   BINDING         24
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P0A8Y5"
FT   BINDING         221
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P0A8Y5"
SQ   SEQUENCE   470 AA;  52223 MW;  46386E388F193A5D CRC64;
     MEESMDAKLK YKAKKIKMVF FDIDDTLRVK DTGYMPESIQ RVFKALKAKG ILVGIASGRA
     RYGVPQEVQD LHADYCVKLN GAYVKDDAKT IIFQAPIPAD VVVAYKKWAD DMGIFYGMAG
     RHEAVLSARN DMISNAIDNV YAQLEVCPDY NEYHDVYQMW TFEDKGDGLQ LPAELAEHLR
     LVRWHDNSSD VVLKGTSKAL GVSKVVDHLG LKPENILVFG DELNDLELFD YAGISIAMGV
     SHPLLQEKAD FITKKVEEDG ILYALEELGL IDKELQFPQL DLENHTGPKV TIKTNHGDMT
     LVLFPDHAPK TVANFLGLAK EGYYDGIIFH RIIPEFMIQG GDPTGTGMGG QSIYGESFED
     EFSDELYNLR GALSMANAGP NTNGSQFFIV QNSKIPYAKK ELERGGWPTP IAAAYAENGG
     TPHLDRRHTV FGQLVDETSF QVLDLIAGVE TGAQDKPKED VIIETIEVFD