ID A0A434AES7_9BACT Unreviewed; 175 AA.
AC A0A434AES7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU003915};
DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU003915};
GN ORFNames=DLK05_16130 {ECO:0000313|EMBL:RUT72893.1};
OS Ancylomarina longa.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinifilaceae;
OC Ancylomarina.
OX NCBI_TaxID=2487017 {ECO:0000313|EMBL:RUT72893.1, ECO:0000313|Proteomes:UP000282985};
RN [1] {ECO:0000313|EMBL:RUT72893.1, ECO:0000313|Proteomes:UP000282985}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T3-2 S1-C {ECO:0000313|EMBL:RUT72893.1,
RC ECO:0000313|Proteomes:UP000282985};
RA Fu T.;
RT "Parancylomarina longa gen. nov., sp. nov., isolated from sediments of
RT southern Okinawa.";
RL Submitted (NOV-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:RUT72893.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; RJJX01000038; RUT72893.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A434AES7; -.
DR OrthoDB; 9808891at2; -.
DR Proteomes; UP000282985; 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:UP000282985};
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 175 AA; 18846 MW; 92ABF8A93DFF49A9 CRC64;
MTIAKDKVIS VIYELKTDPS GEIIEKAVNG TPLTYLCGAG QMLEKFESNL MGLKIGDAFD
FKLESADAYG EASEQAVIDL PKNIFEVNGE LDTEVIKEGN VVPMQDSSGR RMNGIVLEVA
DTTIKMDFNH PLAGDDLYFK GEVIEVREAS EEEMKAAYEP QGGCDGGSCG SGCSC
//
