ID A0A095S5X1_9GAMM Unreviewed; 156 AA.
AC A0A095S5X1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU003915};
DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU003915};
GN ORFNames=T9A_02987 {ECO:0000313|EMBL:KGD60031.1};
OS Alcanivorax jadensis T9.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Alcanivoracaceae; Alcanivorax.
OX NCBI_TaxID=1177181 {ECO:0000313|EMBL:KGD60031.1, ECO:0000313|Proteomes:UP000029443};
RN [1] {ECO:0000313|EMBL:KGD60031.1, ECO:0000313|Proteomes:UP000029443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T9 {ECO:0000313|EMBL:KGD60031.1,
RC ECO:0000313|Proteomes:UP000029443};
RA Lai Q., Shao Z.;
RT "Genome Sequence of alkane-degrading Bacterium Alcanivorax jadensis T9.";
RL Submitted (SEP-2012) 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:KGD60031.1}.
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DR EMBL; ARXU01000015; KGD60031.1; -; Genomic_DNA.
DR RefSeq; WP_035250038.1; NZ_ARXU01000015.1.
DR AlphaFoldDB; A0A095S5X1; -.
DR STRING; 1177181.T9A_02987; -.
DR PATRIC; fig|1177181.3.peg.2966; -.
DR eggNOG; COG1047; Bacteria.
DR OrthoDB; 9808891at2; -.
DR Proteomes; UP000029443; 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; 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:SF4; FKBP-TYPE 16 KDA PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR PANTHER; PTHR47861; 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 10..76
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
SQ SEQUENCE 156 AA; 17275 MW; 38E5943DC282DE16 CRC64;
MTEILRAGPD TRITLHFAVR LMDGTELDST FGGDPAAFVW GDESLLPGFE NALRGLKAGD
RRSVFLEANK AFGDYNDDNV QHFTRSTFAQ YDTLEQGMVL SFADAAGGEL PGVISKVEDE
WVYVDFNHPL AGRDLTFEVE IIAVERYAPE QPVTLN
//