ID A0A0T2IBX9_9MICO Unreviewed; 321 AA.
AC A0A0T2IBX9;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|ARBA:ARBA00013194, ECO:0000256|PROSITE-ProRule:PRU00277};
DE EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194, ECO:0000256|PROSITE-ProRule:PRU00277};
GN ORFNames=ASD62_01265 {ECO:0000313|EMBL:KQZ88154.1};
OS Phycicoccus sp. Root563.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Phycicoccus.
OX NCBI_TaxID=1736562 {ECO:0000313|EMBL:KQZ88154.1, ECO:0000313|Proteomes:UP000051641};
RN [1] {ECO:0000313|Proteomes:UP000051641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root563 {ECO:0000313|Proteomes:UP000051641};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQZ88154.1, ECO:0000313|Proteomes:UP000051641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root563 {ECO:0000313|EMBL:KQZ88154.1,
RC ECO:0000313|Proteomes:UP000051641};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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};
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family.
CC {ECO:0000256|ARBA:ARBA00006577}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQZ88154.1}.
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DR EMBL; LMGM01000001; KQZ88154.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T2IBX9; -.
DR STRING; 1736562.ASD62_01265; -.
DR Proteomes; UP000051641; Unassembled WGS sequence.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.40; -; 2.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR InterPro; IPR006311; TAT_signal.
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.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277};
KW Reference proteome {ECO:0000313|Proteomes:UP000051641};
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..321
FT /note="peptidylprolyl isomerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039361727"
FT DOMAIN 84..173
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT DOMAIN 231..321
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
SQ SEQUENCE 321 AA; 32896 MW; 5A36D4CEA53BFEB0 CRC64;
MRSLSARPSR RRLSVMAAAL TALLALTACG NSDDAKASPL DGITVTGGND TTAPTVAITP
KPLSVKETTT KVVKAGDGPV VKDDEIVSVK YVLLNAKDSS VLDTNYGKQN LGLSLGAEGL
LPGLKKGLAN QKVGSRVLVA VPPKDAFGAQ GNTDIKVGGT DTVVFLMDVL SVTKPLASAE
GKEVKPSADL PSVKVESGKA ATITIPKGKK PPTKTVGQNL IDGTGAKVAA GQTIRVTYTG
ALWKDGKVFD SSATSPQGYF ETVIGKQQVI KAWDAQLVGK AVGSRVLMVV PPADGYGAAG
SPPKISGTDT LVFVVDILAA Y
//
