PPIA_MYCTU
ID PPIA_MYCTU Reviewed; 182 AA.
AC P9WHW3; L0T5F1; P65762; P71578;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase A;
DE Short=PPIase A;
DE EC=5.2.1.8 {ECO:0000269|PubMed:15479239};
DE AltName: Full=Cyclophilin;
DE AltName: Full=Rotamase A;
GN Name=ppiA {ECO:0000303|PubMed:15479239}; OrderedLocusNames=Rv0009;
GN ORFNames=MTCY10H4.08;
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 FUNCTION.
RX PubMed=17141764; DOI=10.1016/j.febslet.2006.11.042;
RA Mitra D., Mukherjee S., Das A.K.;
RT "Cyclosporin A binding to Mycobacterium tuberculosis peptidyl-prolyl cis-
RT trans isomerase A--investigation by CD, FTIR and fluorescence
RT spectroscopy.";
RL FEBS Lett. 580:6846-6860(2006).
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).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 2-182, FUNCTION, CATALYTIC
RP ACTIVITY, AND SUBUNIT.
RC STRAIN=H37Rv;
RX PubMed=15479239; DOI=10.1111/j.1432-1033.2004.04348.x;
RA Henriksson L.M., Johansson P., Unge T., Mowbray S.L.;
RT "X-ray structure of peptidyl-prolyl cis-trans isomerase A from
RT Mycobacterium tuberculosis.";
RL Eur. J. Biochem. 271:4107-4113(2004).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides. {ECO:0000269|PubMed:15479239,
CC ECO:0000269|PubMed:17141764}.
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:0000269|PubMed:15479239};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15479239}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP42731.1; -; Genomic_DNA.
DR PIR; G70698; G70698.
DR RefSeq; NP_214523.1; NC_000962.3.
DR RefSeq; WP_003400321.1; NZ_NVQJ01000005.1.
DR PDB; 1W74; X-ray; 2.60 A; A/B=2-182.
DR PDBsum; 1W74; -.
DR AlphaFoldDB; P9WHW3; -.
DR SMR; P9WHW3; -.
DR STRING; 83332.Rv0009; -.
DR PaxDb; P9WHW3; -.
DR DNASU; 887087; -.
DR GeneID; 45423968; -.
DR GeneID; 887087; -.
DR KEGG; mtu:Rv0009; -.
DR TubercuList; Rv0009; -.
DR eggNOG; COG0652; Bacteria.
DR OMA; ELYNDHA; -.
DR PhylomeDB; P9WHW3; -.
DR BRENDA; 5.2.1.8; 3445.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0005576; C:extracellular region; HDA:MTBBASE.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:MTBBASE.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IBA:GO_Central.
DR GO; GO:0010039; P:response to iron ion; IEP:MTBBASE.
DR Gene3D; 2.40.100.10; -; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR024936; Cyclophilin-type_PPIase.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
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 PIRSF; PIRSF001467; Peptidylpro_ismrse; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; SSF50891; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Isomerase; Reference proteome; Rotamase.
FT CHAIN 1..182
FT /note="Peptidyl-prolyl cis-trans isomerase A"
FT /id="PRO_0000064209"
FT DOMAIN 13..181
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT STRAND 16..21
FT /evidence="ECO:0007829|PDB:1W74"
FT STRAND 24..30
FT /evidence="ECO:0007829|PDB:1W74"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:1W74"
FT HELIX 36..46
FT /evidence="ECO:0007829|PDB:1W74"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:1W74"
FT STRAND 69..75
FT /evidence="ECO:0007829|PDB:1W74"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:1W74"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:1W74"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:1W74"
FT STRAND 109..115
FT /evidence="ECO:0007829|PDB:1W74"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:1W74"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:1W74"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:1W74"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:1W74"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:1W74"
FT HELIX 150..160
FT /evidence="ECO:0007829|PDB:1W74"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:1W74"
FT STRAND 175..182
FT /evidence="ECO:0007829|PDB:1W74"
SQ SEQUENCE 182 AA; 19239 MW; B3D83E7F9486BFCA CRC64;
MADCDSVTNS PLATATATLH TNRGDIKIAL FGNHAPKTVA NFVGLAQGTK DYSTQNASGG
PSGPFYDGAV FHRVIQGFMI QGGDPTGTGR GGPGYKFADE FHPELQFDKP YLLAMANAGP
GTNGSQFFIT VGKTPHLNRR HTIFGEVIDA ESQRVVEAIS KTATDGNDRP TDPVVIESIT
IS
