ID   A0A1X7NN75_9MICO        Unreviewed;       318 AA.
AC   A0A1X7NN75;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU003915};
DE            EC=5.2.1.8 {ECO:0000256|RuleBase:RU003915};
GN   ORFNames=SAMN06295885_1508 {ECO:0000313|EMBL:SMH38511.1};
OS   Rathayibacter oskolensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Rathayibacter.
OX   NCBI_TaxID=1891671 {ECO:0000313|EMBL:SMH38511.1, ECO:0000313|Proteomes:UP000193711};
RN   [1] {ECO:0000313|Proteomes:UP000193711}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM Ac-2121 {ECO:0000313|Proteomes:UP000193711};
RA   Varghese N., Submissions S.;
RL   Submitted (APR-2017) 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|ARBA:ARBA00006577, ECO:0000256|RuleBase:RU003915}.
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DR   EMBL; FXBM01000001; SMH38511.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X7NN75; -.
DR   STRING; 1891671.SAMN06295885_1508; -.
DR   OrthoDB; 25996at2; -.
DR   Proteomes; UP000193711; Unassembled WGS sequence.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.10.50.40; -; 2.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR001179; PPIase_FKBP_dom.
DR   PANTHER; PTHR43811:SF19; 39 KDA FK506-BINDING NUCLEAR PROTEIN; 1.
DR   PANTHER; PTHR43811; FKBP-TYPE PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKPA; 1.
DR   Pfam; PF00254; FKBP_C; 2.
DR   SUPFAM; SSF54534; FKBP-like; 2.
DR   PROSITE; PS50059; FKBP_PPIASE; 2.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..318
FT                   /note="Peptidyl-prolyl cis-trans isomerase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012553005"
FT   DOMAIN          81..170
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50059"
FT   DOMAIN          225..318
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50059"
SQ   SEQUENCE   318 AA;  31708 MW;  EE8A287ECDF08A32 CRC64;
     MRRTVALIAS IGIVAALAGC TASSSVADCD APYGPGDSSA AVDATGDFGY QPDVTVPTPL
     NADGTQVSTL IEGSGDPLEK GQLVTIDYTL VNGADGTVLE ASPYDGESTA RFTVGGAGLI
     GLNEGLLCTQ VGSRVAIAIA PEDGFGDAAS QLGITPEDTL VLVADVQSAS LARADGDPQP
     APNGFPIVTL DENGTPGLAK PSGDAPTDLR IAQLKKGDGA VVEEGDQVVV NYTGWLWSDG
     SVFDSSWENG APAVFTAADG STTQGGVIAG FAEALIGQPV GSQVIAIIPP EDGYGDTAQD
     GIPAGSTIVF VADVLGIA
//