ID A0A2M8RVM0_9PAST Unreviewed; 314 AA.
AC A0A2M8RVM0;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Peptidylprolyl isomerase {ECO:0000313|EMBL:PJG82939.1};
GN ORFNames=CVP04_06135 {ECO:0000313|EMBL:PJG82939.1};
OS Caviibacterium pharyngocola.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Caviibacterium.
OX NCBI_TaxID=28159 {ECO:0000313|EMBL:PJG82939.1, ECO:0000313|Proteomes:UP000230282};
RN [1] {ECO:0000313|EMBL:PJG82939.1, ECO:0000313|Proteomes:UP000230282}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7_3 {ECO:0000313|EMBL:PJG82939.1,
RC ECO:0000313|Proteomes:UP000230282};
RA Christensen H.;
RT "Reclassification of Bisgaard taxon 5 as Caviibacterium pharyngocola gen.
RT nov., sp. nov.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
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:PJG82939.1}.
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; PHGZ01000013; PJG82939.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M8RVM0; -.
DR OrthoDB; 14196at2; -.
DR Proteomes; UP000230282; Unassembled WGS sequence.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-KW.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.40; -; 1.
DR Gene3D; 1.10.4030.10; Porin chaperone SurA, peptide-binding domain; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR000297; PPIase_PpiC.
DR InterPro; IPR023058; PPIase_PpiC_CS.
DR InterPro; IPR015391; SurA_N.
DR InterPro; IPR027304; Trigger_fact/SurA_dom_sf.
DR PANTHER; PTHR47637; CHAPERONE SURA; 1.
DR PANTHER; PTHR47637:SF1; CHAPERONE SURA; 1.
DR Pfam; PF00639; Rotamase; 1.
DR Pfam; PF09312; SurA_N; 1.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR SUPFAM; SSF109998; Triger factor/SurA peptide-binding domain-like; 1.
DR PROSITE; PS01096; PPIC_PPIASE_1; 1.
DR PROSITE; PS50198; PPIC_PPIASE_2; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW ECO:0000313|EMBL:PJG82939.1}; Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Reference proteome {ECO:0000313|Proteomes:UP000230282};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..314
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014915680"
FT DOMAIN 169..269
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 314 AA; 34861 MW; 13B40FEDAE9309C3 CRC64;
MKASHLRAVL FGILGLFAFS TGAQAAERVV ATVNGAPILE SQVKRALGKK ANSEVNRQAA
LNSIIDDILV NQAIKESGVK VNYAQVDRII EGIAAQNGLT FGQLLDALDY QGISYQRYRQ
QIANQLLMSE VRNQAIGKSV DISREEVQEL GQKMLQQARE KGTEKKVTGT EYQTRHILLK
LNPLLNDAQA KAQLSQIRAD IQSGKTTFEQ AALQYSKDYL SGANGGNLGF SFPEAYVEPF
AKAIQTTKKG TISAPFKTEF GWHILEVTDT REGDRTQEAY MQKAYEEIVN KQLKEASKDW
VSALRKHADV KYFN
//
