ID A0A2V2LDH3_9RHOB Unreviewed; 142 AA.
AC A0A2V2LDH3;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU003915};
DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU003915};
GN ORFNames=DKT77_07790 {ECO:0000313|EMBL:PWR03112.1};
OS Meridianimarinicoccus roseus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Meridianimarinicoccus.
OX NCBI_TaxID=2072018 {ECO:0000313|EMBL:PWR03112.1, ECO:0000313|Proteomes:UP000245680};
RN [1] {ECO:0000313|EMBL:PWR03112.1, ECO:0000313|Proteomes:UP000245680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TG-679 {ECO:0000313|EMBL:PWR03112.1,
RC ECO:0000313|Proteomes:UP000245680};
RA Ren Y.;
RT "Rhodobacteraceae gen. nov., sp. nov. isolated from sea water.";
RL Submitted (MAY-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:PWR03112.1}.
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DR EMBL; QGKU01000030; PWR03112.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V2LDH3; -.
DR OrthoDB; 9808891at2; -.
DR Proteomes; UP000245680; 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; 3.10.50.40; -; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
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:UP000245680};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|PROSITE-
KW ProRule:PRU00277}.
FT DOMAIN 7..101
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
SQ SEQUENCE 142 AA; 15060 MW; 9E5AC5FDAB2ED024 CRC64;
MAEVKAGDTV HIHYTGTLND GTTFDSSEGR EPLSFEVGSG QIIPGLDNAL PGMTEGEKKT
VTVASADAYG PVNPEARQPV PREEIPDHIP LDLGTQLQVQ TAEGQTMPVT VAEVTEDTVV
LDANHPLAGQ DLNFDIELVK IA
//
