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Database: UniProt
Entry: A0A1V3JNC3_9PAST
LinkDB: A0A1V3JNC3_9PAST
Original site: A0A1V3JNC3_9PAST 
ID   A0A1V3JNC3_9PAST        Unreviewed;       207 AA.
AC   A0A1V3JNC3;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU003915};
DE            EC=5.2.1.8 {ECO:0000256|RuleBase:RU003915};
GN   ORFNames=BKL49_08510 {ECO:0000313|EMBL:OOF57742.1};
OS   Rodentibacter myodis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Rodentibacter.
OX   NCBI_TaxID=1907939 {ECO:0000313|EMBL:OOF57742.1, ECO:0000313|Proteomes:UP000188602};
RN   [1] {ECO:0000313|EMBL:OOF57742.1, ECO:0000313|Proteomes:UP000188602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ac151 {ECO:0000313|EMBL:OOF57742.1,
RC   ECO:0000313|Proteomes:UP000188602};
RA   Christensen H.;
RT   "Rodentibacter gen. nov. and new species.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:OOF57742.1}.
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DR   EMBL; MLHQ01000022; OOF57742.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V3JNC3; -.
DR   STRING; 1907939.BKL49_08510; -.
DR   OrthoDB; 9814548at2; -.
DR   Proteomes; UP000188602; 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:InterPro.
DR   Gene3D; 3.10.50.40; -; 1.
DR   Gene3D; 1.10.287.460; Peptidyl-prolyl cis-trans isomerase, FKBP-type, N-terminal domain; 1.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR001179; PPIase_FKBP_dom.
DR   InterPro; IPR000774; PPIase_FKBP_N.
DR   InterPro; IPR036944; PPIase_FKBP_N_sf.
DR   PANTHER; PTHR43811:SF23; FKBP-TYPE 22 KDA PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR   PANTHER; PTHR43811; FKBP-TYPE PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKPA; 1.
DR   Pfam; PF00254; FKBP_C; 1.
DR   Pfam; PF01346; FKBP_N; 1.
DR   SUPFAM; SSF54534; FKBP-like; 1.
DR   PROSITE; PS50059; FKBP_PPIASE; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
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          121..207
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50059"
FT   COILED          56..83
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   207 AA;  22392 MW;  69388D7C59C898FD CRC64;
     MSFENVKLES ISEKGSYGIG LQIGQQLLDS QMDIAVEAVA KGIFDALNHN QPALDINDLM
     LSVQQLQQQA AEAQQAQFKV IEEEGKAFLA ENAKKDGVNI TDSGLQYEII TEGNGAKPAA
     TDKVRVHYIG TLPNGTVFDS SVARGQPAEF PVKGVIRGWV EALQMMPVGS KWKLTIPHEL
     AYGERGAGAS IPPFSPLVFE VELLDIL
//
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