ID A0A927KHP4_9XANT Unreviewed; 233 AA.
AC A0A927KHP4;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 02-APR-2025, entry version 9.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU003915};
DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU003915};
GN ORFNames=IB242_02805 {ECO:0000313|EMBL:MBD9367609.1};
OS Xanthomonas sp. XNM01.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Lysobacterales; Lysobacteraceae; Xanthomonas.
OX NCBI_TaxID=2769289 {ECO:0000313|EMBL:MBD9367609.1, ECO:0000313|Proteomes:UP000631838};
RN [1] {ECO:0000313|EMBL:MBD9367609.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=XNM01 {ECO:0000313|EMBL:MBD9367609.1};
RA Gowda K., Ping D., Mani M., Kuehn S.;
RT "A sparse mapping of structure to function in microbial communities.";
RL Submitted (SEP-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}.
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:MBD9367609.1}.
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DR EMBL; JACVAP010000001; MBD9367609.1; -; Genomic_DNA.
DR RefSeq; WP_192275683.1; NZ_JACVAP010000001.1.
DR Proteomes; UP000631838; Unassembled WGS sequence.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR Gene3D; 3.10.50.40; -; 1.
DR Gene3D; 1.10.287.460; Peptidyl-prolyl cis-trans isomerase, FKBP-type, N-terminal domain; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR InterPro; IPR000774; PPIase_FKBP_N.
DR InterPro; IPR036944; PPIase_FKBP_N_sf.
DR Pfam; PF00254; FKBP_C; 1.
DR Pfam; PF01346; FKBP_N; 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 Reference proteome {ECO:0000313|Proteomes:UP000631838};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|PROSITE-
KW ProRule:PRU00277}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..233
FT /note="Peptidyl-prolyl cis-trans isomerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5036860673"
FT DOMAIN 147..233
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
SQ SEQUENCE 233 AA; 25071 MW; 128482A76F78B99C CRC64;
MKLRSIAVAT AALVLAGSAF AQDTTSEKGK LSYYFGYDYG NNLAELADRG EQLDVNSVVK
GVQDALAKKE PAINAEQLRP ALEAFQKREQ ARAEQAKAQY EKVAGENKTR STQFLTQHKA
QAGVQTLAGG IQYRVLEAGN GAKPTQASTV ALEVAGPYPF GQKPEQARPA QQIPAVKVSE
VEMAAMRDVL LQMPAGSKWE VALPPEKAYG ADPRTPFPPN VAVVFEIKLV SVK
//
