ID A0A1X2BZH0_9MYCO Unreviewed; 188 AA.
AC A0A1X2BZH0;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU003915};
DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU003915};
GN ORFNames=AWC23_20215 {ECO:0000313|EMBL:ORW69077.1}, MSAS_09080
GN {ECO:0000313|EMBL:BBX61734.1};
OS Mycobacterium saskatchewanense.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium simiae complex.
OX NCBI_TaxID=220927 {ECO:0000313|EMBL:BBX61734.1, ECO:0000313|Proteomes:UP000467517};
RN [1] {ECO:0000313|EMBL:ORW69077.1, ECO:0000313|Proteomes:UP000193387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44616 {ECO:0000313|EMBL:ORW69077.1,
RC ECO:0000313|Proteomes:UP000193387};
RA Tarcisio F., Conor M., Antonella G., Elisabetta G., Giulia F.S., Sara T.,
RA Anna F., Clotilde B., Roberto B., Veronica D.S., Fabio R., Monica P.,
RA Olivier J., Enrico T., Nicola S.;
RT "The new phylogeny of the genus Mycobacterium.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BBX61734.1, ECO:0000313|Proteomes:UP000467517}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 13016 {ECO:0000313|EMBL:BBX61734.1,
RC ECO:0000313|Proteomes:UP000467517};
RX PubMed=31287781;
RA Matsumoto Y., Kinjo T., Motooka D., Nabeya D., Jung N., Uechi K., Horii T.,
RA Iida T., Fujita J., Nakamura S.;
RT "Comprehensive subspecies identification of 175 nontuberculous mycobacteria
RT species based on 7547 genomic profiles.";
RL Emerg. Microbes Infect. 8:1043-1053(2019).
RN [3] {ECO:0000313|EMBL:BBX61734.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 13016 {ECO:0000313|EMBL:BBX61734.1};
RA Matsumoto Y., Motooka D., Nakamura S.;
RL Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000971, ECO:0000256|PROSITE-
CC ProRule:PRU00277, ECO:0000256|RuleBase:RU003915};
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family.
CC {ECO:0000256|RuleBase:RU003915}.
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DR EMBL; AP022573; BBX61734.1; -; Genomic_DNA.
DR EMBL; LQPR01000049; ORW69077.1; -; Genomic_DNA.
DR STRING; 220927.AWC23_20215; -.
DR KEGG; msak:MSAS_09080; -.
DR OrthoDB; 25996at2; -.
DR Proteomes; UP000193387; Unassembled WGS sequence.
DR Proteomes; UP000467517; Chromosome.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR Pfam; PF00254; FKBP_C; 1.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277,
KW ECO:0000256|RuleBase:RU003915};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|PROSITE-
KW ProRule:PRU00277}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..188
FT /note="Peptidyl-prolyl cis-trans isomerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041085198"
FT DOMAIN 100..187
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
SQ SEQUENCE 188 AA; 18570 MW; DDC5211C7E9C154D CRC64;
MAAVKLFRTY PTVALTACVA ATVCTLATSG TAAAAGSCPT AAPPAGGSPE WTLAGTTGSI
GVTGSTDTTA PRVNVTTPFS VTQTQVHTLR AGDGPVVPAT ARVSVCYMGV NGRDGSVFDS
SYDRGAPVDF PLNGVVPGFQ KAIAGQTVGS TVAVAMTSAD GYPDGQPSAG IRPGDSLVFA
IKILSASS
//
