ID   PPIB_MYCTU              Reviewed;         308 AA.
AC   P9WHW1; L0TCU5; Q50639;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=Probable peptidyl-prolyl cis-trans isomerase B;
DE            Short=PPIase B;
DE            EC=5.2.1.8;
DE   AltName: Full=Rotamase B;
GN   Name=ppiB; Synonyms=ppi; OrderedLocusNames=Rv2582; ORFNames=MTCY227.19c;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX   PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA   Raman K., Yeturu K., Chandra N.;
RT   "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT   through an interactome, reactome and genome-scale structural analysis.";
RL   BMC Syst. Biol. 2:109-109(2008).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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}.
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   -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC       {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; AL123456; CCP45378.1; -; Genomic_DNA.
DR   PIR; E70725; E70725.
DR   RefSeq; NP_217098.1; NC_000962.3.
DR   RefSeq; WP_003413367.1; NC_000962.3.
DR   AlphaFoldDB; P9WHW1; -.
DR   SMR; P9WHW1; -.
DR   STRING; 83332.Rv2582; -.
DR   PaxDb; P9WHW1; -.
DR   DNASU; 887691; -.
DR   GeneID; 887691; -.
DR   KEGG; mtu:Rv2582; -.
DR   PATRIC; fig|83332.111.peg.2885; -.
DR   TubercuList; Rv2582; -.
DR   eggNOG; COG0652; Bacteria.
DR   OMA; SKAPDPC; -.
DR   PhylomeDB; P9WHW1; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; HDA:MTBBASE.
DR   GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR   GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IBA:GO_Central.
DR   Gene3D; 2.40.100.10; -; 1.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   InterPro; IPR044666; Cyclophilin_A-like.
DR   PANTHER; PTHR45625; PTHR45625; 1.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SUPFAM; SSF50891; SSF50891; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
PE   1: Evidence at protein level;
KW   Isomerase; Reference proteome; Rotamase.
FT   CHAIN           1..308
FT                   /note="Probable peptidyl-prolyl cis-trans isomerase B"
FT                   /id="PRO_0000064212"
FT   DOMAIN          139..307
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   REGION          74..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        74..93
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   308 AA;  32371 MW;  270222818C2485BF CRC64;
     MGHLTPVAAP RLACAFVPTN AQRRATAKRK LERQLERRAK QAKRRRILTI VGGSLAAVAV
     IVAVVVTVVV NKDDHQSTTS ATPTDSASTS PPQAATAPPL PPFKPSANLG ANCQYPPSPD
     KAVKPVKLPR TGKVPTDPAQ VSVSMVTNQG NIGLMLANNE SPCTVNSFVS LAQQGFFKGT
     TCHRLTTSPM LAVLQCGDPK GDGTGGPGYQ FANEYPTDQY SANDPKLNEP VIYPRGTLAM
     ANAGPNTNSS QFFMVYRDSK LPPQYTVFGT IQADGLTTLD KIAKAGVAGG GEDGKPATEV
     TITSVLLD