ID A0A246K0M6_9SPHN Unreviewed; 183 AA.
AC A0A246K0M6;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU003915};
DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU003915};
GN ORFNames=CDQ92_01600 {ECO:0000313|EMBL:OWQ98911.1};
OS Sphingopyxis bauzanensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=651663 {ECO:0000313|EMBL:OWQ98911.1, ECO:0000313|Proteomes:UP000197361};
RN [1] {ECO:0000313|EMBL:OWQ98911.1, ECO:0000313|Proteomes:UP000197361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22271 {ECO:0000313|EMBL:OWQ98911.1,
RC ECO:0000313|Proteomes:UP000197361};
RX PubMed=20023054; DOI=10.1099/ijs.0.018218-0;
RA Zhang D.C., Liu H.C., Xin Y.H., Zhou Y.G., Schinner F., Margesin R.;
RT "Sphingopyxis bauzanensis sp. nov., a psychrophilic bacterium isolated from
RT soil.";
RL Int. J. Syst. Evol. Microbiol. 60:2618-2622(2010).
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:OWQ98911.1}.
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DR EMBL; NISK01000001; OWQ98911.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A246K0M6; -.
DR OrthoDB; 9812109at2; -.
DR Proteomes; UP000197361; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006457; P:protein folding; IEA:UniProt.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR PANTHER; PTHR43811:SF19; 39 KDA FK506-BINDING NUCLEAR PROTEIN; 1.
DR PANTHER; PTHR43811; FKBP-TYPE PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKPA; 1.
DR Pfam; PF00254; FKBP_C; 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}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000197361};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|PROSITE-
KW ProRule:PRU00277}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 57..138
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT REGION 149..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 183 AA; 19593 MW; 4DD5F0A17A156D08 CRC64;
MSVTTVPLRP VNNKGLWLIW IGVIALLGAA AAFAYHVTPR IGFEVIKEGT GKSPTKADVV
LVKYEGKLDD GTVFDANEQA PMQVAQVVPG FSEALTRMKK GGQYKIIIPP QLGYGDREAG
PIPAGSTLHF DVTLLDFRSE AEVRAMQQQM QQQQQMMQQQ QMMQGAPGGA GPAGPPPGAP
PQP
//
