ID A0A060REW7_9BACT Unreviewed; 183 AA.
AC A0A060REW7;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU003915};
DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU003915};
GN ORFNames=BN938_3017 {ECO:0000313|EMBL:CDN33079.1};
OS Mucinivorans hirudinis.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC Mucinivorans.
OX NCBI_TaxID=1433126 {ECO:0000313|EMBL:CDN33079.1, ECO:0000313|Proteomes:UP000027616};
RN [1] {ECO:0000313|EMBL:CDN33079.1, ECO:0000313|Proteomes:UP000027616}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M3 {ECO:0000313|Proteomes:UP000027616};
RX PubMed=25657285; DOI=10.1128/genomeA.01530-14;
RA Nelson M.C., Bomar L., Graf J.;
RT "Complete Genome Sequence of the Novel Leech Symbiont Mucinivorans
RT hirudinis M3T.";
RL Genome Announc. 3:e01530-e01514(2015).
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}.
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DR EMBL; HG934468; CDN33079.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A060REW7; -.
DR STRING; 1433126.BN938_3017; -.
DR KEGG; rbc:BN938_3017; -.
DR PATRIC; fig|1433126.3.peg.2985; -.
DR eggNOG; COG1047; Bacteria.
DR HOGENOM; CLU_098197_0_0_10; -.
DR OrthoDB; 9808891at2; -.
DR Proteomes; UP000027616; Chromosome I.
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:UP000027616};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|PROSITE-
KW ProRule:PRU00277}.
FT DOMAIN 6..85
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
SQ SEQUENCE 183 AA; 19607 MW; F0F7784D39AA616C CRC64;
MNITENKLVK LAYELKVDGE IADKATAERP LEFIFGTGML LPDFEANVEG KVAGDKFAFT
LTPEQGYGEI NNEAVVELPK EIFMVDGVVA DELLVVGSVL PMGDNMGNRM NGVIKDVKDD
VVVMDFNHPM AGKILNFSGE IVEVREATDE DTAKFFGGSG GGCGCGCDKS ECDSNDCSSD
CNC
//
