ID A0A0Q5V0E3_9CAUL Unreviewed; 175 AA.
AC A0A0Q5V0E3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 18-JUN-2025, entry version 38.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU003915};
DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU003915};
GN ORFNames=ASG17_03200 {ECO:0000313|EMBL:KQS55120.1};
OS Brevundimonas sp. Leaf363.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Caulobacterales; Caulobacteraceae; Brevundimonas.
OX NCBI_TaxID=1736353 {ECO:0000313|EMBL:KQS55120.1, ECO:0000313|Proteomes:UP000051182};
RN [1] {ECO:0000313|EMBL:KQS55120.1, ECO:0000313|Proteomes:UP000051182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf363 {ECO:0000313|EMBL:KQS55120.1,
RC ECO:0000313|Proteomes:UP000051182};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQS55120.1, ECO:0000313|Proteomes:UP000051182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf363 {ECO:0000313|EMBL:KQS55120.1,
RC ECO:0000313|Proteomes:UP000051182};
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, ECO:0000256|RuleBase:RU003915};
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family.
CC {ECO:0000256|RuleBase:RU003915}.
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:KQS55120.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMPZ01000002; KQS55120.1; -; Genomic_DNA.
DR RefSeq; WP_056099108.1; NZ_LMPZ01000002.1.
DR AlphaFoldDB; A0A0Q5V0E3; -.
DR STRING; 1736353.ASG17_03200; -.
DR OrthoDB; 9812109at2; -.
DR Proteomes; UP000051182; Unassembled WGS sequence.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IEA:InterPro.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR044609; FKBP2/11.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR InterPro; IPR000774; PPIase_FKBP_N.
DR PANTHER; PTHR45779; PEPTIDYLPROLYL ISOMERASE; 1.
DR PANTHER; PTHR45779:SF7; PEPTIDYLPROLYL ISOMERASE; 1.
DR Pfam; PF00254; FKBP_C; 1.
DR Pfam; PF01346; FKBP_N; 1.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|PROSITE-
KW ProRule:PRU00277}; Reference proteome {ECO:0000313|Proteomes:UP000051182};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|PROSITE-
KW ProRule:PRU00277}.
FT DOMAIN 74..160
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
SQ SEQUENCE 175 AA; 18071 MW; DB5F8E7857937408 CRC64;
MRFGWVSVAV VAVLATAACK KTEAPAGDGA EQAAAARFFL ESNGRAEGVT TLPSGLQYKV
VQSGPPGGES PDRNDLVRVD YEGALTDGRV FDSSYQRGAP AVFTPETVVP GWTEALQHMK
VGDEWVLYVP PALGYGEEGA PPTIPGNAVL VFKLKLLDLA RVPGGGSAGV GSANG
//
