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Database: UniProt
Entry: A0A2A3LJA7_9GAMM
LinkDB: A0A2A3LJA7_9GAMM
Original site: A0A2A3LJA7_9GAMM 
ID   A0A2A3LJA7_9GAMM        Unreviewed;       156 AA.
AC   A0A2A3LJA7;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-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=CMZ84_00500 {ECO:0000313|EMBL:PBJ83078.1};
OS   Xanthomonadaceae bacterium NML93-0399.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae.
OX   NCBI_TaxID=2032565 {ECO:0000313|EMBL:PBJ83078.1, ECO:0000313|Proteomes:UP000218035};
RN   [1] {ECO:0000313|EMBL:PBJ83078.1, ECO:0000313|Proteomes:UP000218035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NML93-0399 {ECO:0000313|EMBL:PBJ83078.1,
RC   ECO:0000313|Proteomes:UP000218035};
RA   Bernier A.-M., Bernard K.;
RT   "Clinical and environmental strains of Xanthomonadaceae.";
RL   Submitted (SEP-2017) 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:PBJ83078.1}.
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DR   EMBL; NTJI01000001; PBJ83078.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A3LJA7; -.
DR   OrthoDB; 9808891at2; -.
DR   Proteomes; UP000218035; Unassembled WGS sequence.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006457; P:protein folding; 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   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   156 AA;  16513 MW;  D163D35073B37D55 CRC64;
     MEIAAARVAT FHYTLTDDDG NVIDSSKNAS PLPYFHGGGN IVPGLEKALE GRKAGDTLNV
     DVQPEEGYGL RNDSLVQAVP RQAFQGIDTI EPGMQFQAQG GAGPMLVTVV EVGDTEVKID
     GNHPLAGKTL HFAIEVVDVR ESTDDEKQAG QVARAA
//
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