ID A0A7W9R4K6_9SPHN Unreviewed; 447 AA. AC A0A7W9R4K6; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 29-SEP-2021, entry version 2. DE RecName: Full=Parvulin-like PPIase {ECO:0000256|ARBA:ARBA00018370}; DE AltName: Full=Peptidyl-prolyl cis-trans isomerase plp {ECO:0000256|ARBA:ARBA00015258}; DE AltName: Full=Rotamase plp {ECO:0000256|ARBA:ARBA00013748}; GN ORFNames=HNP59_001192 {ECO:0000313|EMBL:MBB5969429.1}; OS Sphingobium sp. B12D2A. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingobium. OX NCBI_TaxID=2735885 {ECO:0000313|EMBL:MBB5969429.1, ECO:0000313|Proteomes:UP000570197}; RN [1] {ECO:0000313|EMBL:MBB5969429.1, ECO:0000313|Proteomes:UP000570197} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B12D2A {ECO:0000313|EMBL:MBB5969429.1, RC ECO:0000313|Proteomes:UP000570197}; RA Elkins J.; RT "Exploring microbial biodiversity for novel pathways involved in the RT catabolism of aromatic compounds derived from lignin."; RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the PpiC/parvulin rotamase family. CC {ECO:0000256|ARBA:ARBA00007656}. 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:MBB5969429.1}. 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; JACHJZ010000001; MBB5969429.1; -; Genomic_DNA. DR Proteomes; UP000570197; Unassembled WGS sequence. DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-EC. DR InterPro; IPR000297; PPIase_PpiC. DR InterPro; IPR015391; SurA_N. DR InterPro; IPR027304; Trigger_fact/SurA_dom_sf. DR Pfam; PF00639; Rotamase; 1. DR Pfam; PF09312; SurA_N; 1. DR SUPFAM; SSF109998; SSF109998; 1. DR PROSITE; PS50198; PPIC_PPIASE_2; 1. PE 3: Inferred from homology; KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278, KW ECO:0000313|EMBL:MBB5969429.1}; Periplasm {ECO:0000256|ARBA:ARBA00022764}; KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..21 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 22..447 FT /note="Parvulin-like PPIase" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5030675767" FT DOMAIN 199..296 FT /note="PpiC" FT /evidence="ECO:0000259|PROSITE:PS50198" SQ SEQUENCE 447 AA; 48166 MW; F5A43941D3EBC701 CRC64; MPSGIARAVI ASVATCLIVQ AAPSQTVGGD DLNAPSTALD IPADVTMFGK RDPNVRKATA LVNGEVITET DIEQRLALVV LANGGKVSAE ETDRLRLQVL RNLIDETLQI QEAAAKDIRV PKAELDENFA RVAANFRYSP EGFAKYLGEH GSSERSIKRQ IEGEVAWNRL LRREVQPFVN VSEDEVTAIV DRLKASKGKD EFHVGEIYLS ATPETTQQVQ ANGEQIMEQI RKGGSFQAYA RQYSEASTAA VGGDLGWVRP AQLPDALASA VQQLEVGQVV GPIPIPGGFS ILYLVDKRQV LTADPRDAVL SLKQLAIDFP PGTTPAQAQQ KANAFGDALS KLQGCGAVSE LAQGLGATVV ENDIVARNLP PQLQSVLLAM QVGEATPPFG SATEGVRALI LCGRDDPQDA GSPSFDQIMS QMEEDRVNKR ARTYLRDLRR DAVIDYN //