ID H8KN44_SOLCM Unreviewed; 293 AA.
AC H8KN44;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU003915};
DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU003915};
GN OrderedLocusNames=Solca_4387 {ECO:0000313|EMBL:AFD09377.1};
OS Solitalea canadensis (strain ATCC 29591 / DSM 3403 / NBRC 15130 / NCIMB
OS 12057 / USAM 9D) (Flexibacter canadensis).
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Solitalea.
OX NCBI_TaxID=929556 {ECO:0000313|EMBL:AFD09377.1, ECO:0000313|Proteomes:UP000007590};
RN [1] {ECO:0000313|Proteomes:UP000007590}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29591 / DSM 3403 / NBRC 15130 / NCIMB 12057 / USAM 9D
RC {ECO:0000313|Proteomes:UP000007590};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Lu M.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Spring S., Schroeder M., Kopitz M., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "The complete genome of Solitalea canadensis DSM 3403.";
RL Submitted (FEB-2012) 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|RuleBase:RU003915}.
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DR EMBL; CP003349; AFD09377.1; -; Genomic_DNA.
DR RefSeq; WP_014682599.1; NC_017770.1.
DR AlphaFoldDB; H8KN44; -.
DR STRING; 929556.Solca_4387; -.
DR KEGG; scn:Solca_4387; -.
DR eggNOG; COG0545; Bacteria.
DR HOGENOM; CLU_047811_0_0_10; -.
DR OrthoDB; 9814548at2; -.
DR Proteomes; UP000007590; Chromosome.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.10.50.40; -; 2.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR PANTHER; PTHR10516; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR PANTHER; PTHR10516:SF464; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKBP12; 1.
DR Pfam; PF00254; FKBP_C; 1.
DR SUPFAM; SSF54534; FKBP-like; 2.
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:UP000007590};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|PROSITE-
KW ProRule:PRU00277}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..293
FT /note="Peptidyl-prolyl cis-trans isomerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003613211"
FT DOMAIN 202..290
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
SQ SEQUENCE 293 AA; 32356 MW; 0BB1EDDF55EE4BDA CRC64;
MKQLKFLIAL LVIAGVTLMA FDNGFQQTKR GLFYKILKTT ATNKIKIKQG DYVKFHMIYK
TDKDSILQST YKLKQPAEVI VRIDTMADKS QVMEALTLLA KGDSATFRIG SDLLFKGAPA
SVQRPPFLAS KRFLCYTIKV IDVKTPQQME AEAKAAAAKR KAEEDKSISD YAKVNNLQLS
TTPSGLRYQI TSKGNGVNAK AGDTINVHYT GKLLSGKKFD SSYDRNQPIE FMLGKNMVIA
GWDEGLQLLK KGEKAVFVIP SGLAYGERAM GADIPANSIL VFDVELVDIK PVK
//
