ID A5G4S2_GEOUR Unreviewed; 421 AA.
AC A5G4S2;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|PROSITE-ProRule:PRU00277};
DE EC=5.2.1.8 {ECO:0000256|PROSITE-ProRule:PRU00277};
GN OrderedLocusNames=Gura_2613 {ECO:0000313|EMBL:ABQ26790.1};
OS Geotalea uraniireducens (strain Rf4) (Geobacter uraniireducens).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC Geobacteraceae; Geotalea.
OX NCBI_TaxID=351605 {ECO:0000313|EMBL:ABQ26790.1, ECO:0000313|Proteomes:UP000006695};
RN [1] {ECO:0000313|EMBL:ABQ26790.1, ECO:0000313|Proteomes:UP000006695}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rf4 {ECO:0000313|EMBL:ABQ26790.1,
RC ECO:0000313|Proteomes:UP000006695};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Shelobolina E., Aklujkar M.,
RA Lovley D., Richardson P.;
RT "Complete sequence of Geobacter uraniireducens Rf4.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Also involved in hydrogenase metallocenter assembly, probably
CC by participating in the nickel insertion step. This function in
CC hydrogenase biosynthesis requires chaperone activity and the presence
CC of the metal-binding domain, but not PPIase activity.
CC {ECO:0000256|ARBA:ARBA00037071}.
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};
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family.
CC {ECO:0000256|ARBA:ARBA00006577}.
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DR EMBL; CP000698; ABQ26790.1; -; Genomic_DNA.
DR AlphaFoldDB; A5G4S2; -.
DR STRING; 351605.Gura_2613; -.
DR KEGG; gur:Gura_2613; -.
DR HOGENOM; CLU_677495_0_0_7; -.
DR OrthoDB; 9811036at2; -.
DR Proteomes; UP000006695; Chromosome.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0042026; P:protein refolding; IEA:UniProt.
DR CDD; cd02947; TRX_family; 1.
DR Gene3D; 3.10.50.40; -; 2.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR47861; FKBP-TYPE PEPTIDYL-PROLYL CIS-TRANS ISOMERASE SLYD; 1.
DR PANTHER; PTHR47861:SF3; FKBP-TYPE PEPTIDYL-PROLYL CIS-TRANS ISOMERASE SLYD; 1.
DR Pfam; PF00254; FKBP_C; 1.
DR Pfam; PF13899; Thioredoxin_7; 1.
DR SUPFAM; SSF54534; FKBP-like; 2.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277,
KW ECO:0000313|EMBL:ABQ26790.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006695};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|PROSITE-
KW ProRule:PRU00277}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..421
FT /note="peptidylprolyl isomerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002683234"
FT DOMAIN 88..186
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT DOMAIN 287..420
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 421 AA; 45128 MW; FD65C7585576A980 CRC64;
MNMNHCQRII SSHAVKRSLV ILAAVSALAG CAGQPLKSAA VQETPPAAGT NQAASPEKAN
AALDEAVKSG RTTASIDLNE TPGTVQKGDV VTVDYTVTDA AGKLLRTSRA AVANDPGQRL
APEEIIAGTP AAIPGLGEAV PGMAIGGKKS VKLPAEKAFG LSDPAKIFQF PTVKTISKTI
RMPADEYVKQ FGAFPVVGKE LELAPYFKSR ITAVSEKEAT LEFLAKDGER FTEPYGEVQV
RLDGEQISIN IAPRIGAPLE VQGKRGTITA VDAASFTADF NHPLAGKDIT LDLEVVSLVK
ASALGKHAIT WLEDHDKGLS AAKENGTPAV LVLYAEWCGW CKKLFEESVQ DPRVRLLSDR
FVWLKVNSNK EQKFKAQYGQ DGFPLIVVLD RDGREATRID GFRDGEALSR ELRAVTENLK
I
//
