ID A0A927Q9X7_9XANT Unreviewed; 310 AA.
AC A0A927Q9X7;
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_10605 {ECO:0000313|EMBL:MBD9369130.1};
OS Xanthomonas sp. XNM01.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Lysobacterales; Lysobacteraceae; Xanthomonas.
OX NCBI_TaxID=2769289 {ECO:0000313|EMBL:MBD9369130.1, ECO:0000313|Proteomes:UP000631838};
RN [1] {ECO:0000313|EMBL:MBD9369130.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=XNM01 {ECO:0000313|EMBL:MBD9369130.1};
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|ARBA:ARBA00006577, 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:MBD9369130.1}.
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DR EMBL; JACVAP010000002; MBD9369130.1; -; Genomic_DNA.
DR RefSeq; WP_192278943.1; NZ_JACVAP010000002.1.
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 FunFam; 3.10.50.40:FF:000006; Peptidyl-prolyl cis-trans isomerase; 1.
DR Gene3D; 3.10.50.40; -; 1.
DR Gene3D; 1.10.287.460; Peptidyl-prolyl cis-trans isomerase, FKBP-type, N-terminal domain; 2.
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 PANTHER; PTHR43811; FKBP-TYPE PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKPA; 1.
DR PANTHER; PTHR43811:SF57; FKBP-TYPE PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKPA-RELATED; 1.
DR Pfam; PF00254; FKBP_C; 1.
DR Pfam; PF01346; FKBP_N; 2.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|PROSITE-
KW ProRule:PRU00277}; 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..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..310
FT /note="Peptidyl-prolyl cis-trans isomerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5037895934"
FT DOMAIN 222..309
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
SQ SEQUENCE 310 AA; 32529 MW; 1EEFFAF66F295752 CRC64;
MNNRVRGAMA SLMMGASMMA GVAVAQDKTV LATEKDKVSY AIGLDVARSF EPIAQDIDVA
ALERAVGNAL AGKEPLQSEE QARATDAALR TALAARSGQR VPGMAPGSEP QAPSKDQVGL
LVGDRMVGPS LQPLKDDIDP AVLFQAVRTA LAKGTPLLNE QEAMATLQAF MTRKQSAVGD
KNRADGAAFL AENGKQKGVI TTPSGLQYQV LREGSGQRPV ASDTVRVNYE GKLLDGTVFD
SSYARGEAIE FGLGQVIRGW TEGVSLMPVG AKYRFWIPSD LAYGPNGAPG GKIGPNATLT
FDVELLGIAP
//
