ID A0A2T0WS29_9BACT Unreviewed; 175 AA.
AC A0A2T0WS29;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU003915};
DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU003915};
GN ORFNames=DFO77_13723 {ECO:0000313|EMBL:RCW27491.1};
OS Marinilabilia salmonicolor.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinilabiliaceae;
OC Marinilabilia.
OX NCBI_TaxID=989 {ECO:0000313|EMBL:RCW27491.1, ECO:0000313|Proteomes:UP000252733};
RN [1] {ECO:0000313|EMBL:RCW27491.1, ECO:0000313|Proteomes:UP000252733}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=160A {ECO:0000313|EMBL:RCW27491.1,
RC ECO:0000313|Proteomes:UP000252733};
RA Lamendella R.;
RT "Freshwater and sediment microbial communities from various areas in North
RT America, analyzing microbe dynamics in response to fracking.";
RL Submitted (JUL-2018) 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:RCW27491.1}.
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DR EMBL; QPIZ01000037; RCW27491.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0WS29; -.
DR STRING; 1168289.GCA_000259075_02291; -.
DR OrthoDB; 9808891at2; -.
DR Proteomes; UP000252733; 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 Reference proteome {ECO:0000313|Proteomes:UP000252733};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|PROSITE-
KW ProRule:PRU00277}.
FT DOMAIN 6..84
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
SQ SEQUENCE 175 AA; 18982 MW; 96912DE3517ABA0D CRC64;
MEIARNKFVS LSYQLRLNGA EGDLVEETGE NNPLQFVYGA GKMIEMFEKK IEGLKQGDNF
KFELKADEAY GQVNTEAIVD LPKNIFEVEG KIDESLLKIG NMVPMQDANG NRLNGIVLEV
TDDTVKMDFN HPLAGDDLHF AGQVLEVRDA TENELVEAVG GGGCSSGSCG DGCSC
//
