ID A0A1E5IQH5_SHECO Unreviewed; 205 AA.
AC A0A1E5IQH5;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU003915};
DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU003915};
GN ORFNames=BEL05_11110 {ECO:0000313|EMBL:OEG72811.1};
OS Shewanella colwelliana (Alteromonas colwelliana).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=23 {ECO:0000313|EMBL:OEG72811.1, ECO:0000313|Proteomes:UP000095230};
RN [1] {ECO:0000313|EMBL:OEG72811.1, ECO:0000313|Proteomes:UP000095230}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSB03KR {ECO:0000313|EMBL:OEG72811.1,
RC ECO:0000313|Proteomes:UP000095230};
RA Hong H.-H., Choi H., Cheon S., Oh J.-S., Lee H.-G., Park C.;
RT "Whole-genome of two Shewanella species isolated from a digestive organ of
RT sea cucumber Apostichopus japonicus Selenka 1867.";
RL Submitted (JUL-2016) 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, 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:OEG72811.1}.
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DR EMBL; MCBT01000046; OEG72811.1; -; Genomic_DNA.
DR RefSeq; WP_069671888.1; NZ_MCBT01000046.1.
DR AlphaFoldDB; A0A1E5IQH5; -.
DR STRING; 23.BEL05_11110; -.
DR OrthoDB; 9808891at2; -.
DR Proteomes; UP000095230; Unassembled WGS sequence.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042026; P:protein refolding; IEA:UniProt.
DR Gene3D; 2.40.10.330; -; 1.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR InterPro; IPR048261; SlpA/SlyD-like_ins_sf.
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 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};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|PROSITE-
KW ProRule:PRU00277}.
FT DOMAIN 6..83
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
SQ SEQUENCE 205 AA; 21836 MW; 9D6B480948EE7AF0 CRC64;
MIITQHTAVS IHYRLTNQQG ELVESSFEGE PMLYLHGAEN MIPGLEEALE GKSVGDKLDV
TIEAEKAYGA YHDGLRQEVP LSAFGDIEDI VPGMRFIAET EMGQRPVQVT EVKDEVVVVD
GNHPLAGQSL NFSVEVLAVR EATAEEISHG HIHAHGGSCG GHEHSHEGGC CGGEGHSHEG
GCCNDDADKE PKEGCDGNGG CGCRH
//
