ID A0A0A7EHX8_9GAMM Unreviewed; 205 AA.
AC A0A0A7EHX8;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, 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=OM33_11155 {ECO:0000313|EMBL:AIY65651.1};
OS Pseudoalteromonas piratica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=1348114 {ECO:0000313|EMBL:AIY65651.1, ECO:0000313|Proteomes:UP000030341};
RN [1] {ECO:0000313|EMBL:AIY65651.1, ECO:0000313|Proteomes:UP000030341}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OCN003 {ECO:0000313|EMBL:AIY65651.1,
RC ECO:0000313|Proteomes:UP000030341};
RA Beurmann S., Videau P., Ushijima B., Smith A.M., Aeby G.S., Callahan S.M.,
RA Belcaid M.;
RT "Complete Genome Sequence of Pseudoalteromonas sp. Strain OCN003 Isolated
RT from Kaneohe Bay, Oahu, Hawaii.";
RL Submitted (NOV-2014) 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}.
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DR EMBL; CP009888; AIY65651.1; -; Genomic_DNA.
DR RefSeq; WP_038641726.1; NZ_CP009888.1.
DR AlphaFoldDB; A0A0A7EHX8; -.
DR STRING; 1348114.OM33_11155; -.
DR KEGG; pseo:OM33_11155; -.
DR eggNOG; COG0545; Bacteria.
DR HOGENOM; CLU_013615_0_1_6; -.
DR OrthoDB; 9814548at2; -.
DR Proteomes; UP000030341; Chromosome 1.
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 Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277,
KW ECO:0000256|RuleBase:RU003915};
KW Reference proteome {ECO:0000313|Proteomes:UP000030341};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|PROSITE-
KW ProRule:PRU00277}.
FT DOMAIN 119..205
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
SQ SEQUENCE 205 AA; 22232 MW; FD63C276CC9BF211 CRC64;
MSDKFNSNAE KASYGIGLQM GEQLKSNPFE GLNLNSVFEG MKDAYTGGEF QVEIPAIQAA
FEEINAEITK RREEEAKVLA AEGESFLAEN AKRAEVTVTA SGLQYEVLTA GEGDKPTAES
TVRTHYHGTL INGEVFDSSY DRGQPAEFPV GGVIKGWTEA LQMMPVGSKW RLYVPHDLAY
GERGAGASIA PFSTLIFDVE LLAIV
//
