PPIB_MYCTO
ID PPIB_MYCTO Reviewed; 308 AA.
AC P9WHW0; L0TCU5; Q50639;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 40.
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=MT2659;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
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 -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000305}.
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DR EMBL; AE000516; AAK46972.1; -; Genomic_DNA.
DR PIR; E70725; E70725.
DR RefSeq; WP_003413367.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WHW0; -.
DR SMR; P9WHW0; -.
DR EnsemblBacteria; AAK46972; AAK46972; MT2659.
DR KEGG; mtc:MT2659; -.
DR PATRIC; fig|83331.31.peg.2866; -.
DR HOGENOM; CLU_012062_8_0_11; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
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 3: Inferred from homology;
KW Isomerase; Rotamase.
FT CHAIN 1..308
FT /note="Probable peptidyl-prolyl cis-trans isomerase B"
FT /id="PRO_0000428113"
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
