ID E7BMF0_9GAMM Unreviewed; 209 AA. AC E7BMF0; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 12-AUG-2020, entry version 35. DE RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU003915}; DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU003915}; DE Flags: Fragment; GN Name=mip {ECO:0000313|EMBL:ADR82239.1}; OS Legionella sp. ST19309. OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Legionellaceae; Legionella; unclassified Legionella. OX NCBI_TaxID=907839 {ECO:0000313|EMBL:ADR82239.1}; RN [1] {ECO:0000313|EMBL:ADR82239.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ST19309 {ECO:0000313|EMBL:ADR82239.1}; RX PubMed=22504352; DOI=10.1016/j.meegid.2012.03.025; RA Paveenkittiporn W., Dejsirilert S., Kalambaheti T.; RT "Genetic speciation of environmental Legionella isolates in Thailand."; RL Infect. Genet. Evol. 12:1368-1376(2012). CC -!- FUNCTION: Essential virulence factor associated with macrophage CC infectivity. Exhibits PPIase activity. {ECO:0000256|ARBA:ARBA00002861}. 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 -!- SUBCELLULAR LOCATION: Cell outer membrane CC {ECO:0000256|ARBA:ARBA00004442}. Membrane CC {ECO:0000256|ARBA:ARBA00004370}. CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. CC {ECO:0000256|ARBA:ARBA00006577, ECO:0000256|RuleBase:RU003915}. 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; GU083723; ADR82239.1; -; Genomic_DNA. DR GO; GO:0016020; C:membrane; IEA:InterPro. 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; 1.10.287.460; -; 1. DR InterPro; IPR008104; INFPOTNTIATR. 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 PRINTS; PR01730; INFPOTNTIATR. DR PROSITE; PS50059; FKBP_PPIASE; 1. PE 3: Inferred from homology; KW Cell outer membrane {ECO:0000256|ARBA:ARBA00023237}; KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277, KW ECO:0000256|RuleBase:RU003915}; Membrane {ECO:0000256|ARBA:ARBA00023237}; KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|PROSITE- KW ProRule:PRU00277, ECO:0000256|RuleBase:RU003915}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}; KW Virulence {ECO:0000256|ARBA:ARBA00023026}. FT SIGNAL 1..19 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 20..209 FT /note="Peptidyl-prolyl cis-trans isomerase" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5003216019" FT DOMAIN 142..209 FT /note="PPIase FKBP-type" FT /evidence="ECO:0000259|PROSITE:PS50059" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:ADR82239.1" FT NON_TER 209 FT /evidence="ECO:0000313|EMBL:ADR82239.1" SQ SEQUENCE 209 AA; 22262 MW; 5EB24656BFDD7389 CRC64; KMRLVTAAVM GLAMSTVIAA DATSLVTDKD KLSYSIGADL GKNFKNQGID INPDALAKGM QDGMSGAQLI LTEQQMKDVL NKFQKELMAK RSAEFNKKAE ENKSKGDAFL STNKSKSGVT VLPSGLQYKV IEAGTGNKPG KADTVTVEYT GTLIDGTVFD STEKTGKPAT FQVSQVIPGW TEALQLMPAG STWEIYVPSD LAYGPRSVG //