ID Q82Y46_NITEU Unreviewed; 213 AA.
AC Q82Y46;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 129.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU363019};
DE Short=PPIase {ECO:0000256|RuleBase:RU363019};
DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU363019};
GN Name=ppiA {ECO:0000313|EMBL:CAD83953.1};
GN OrderedLocusNames=NE0042 {ECO:0000313|EMBL:CAD83953.1};
OS Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC
OS 14298).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=228410 {ECO:0000313|EMBL:CAD83953.1, ECO:0000313|Proteomes:UP000001416};
RN [1] {ECO:0000313|EMBL:CAD83953.1, ECO:0000313|Proteomes:UP000001416}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298
RC {ECO:0000313|Proteomes:UP000001416};
RX PubMed=12700255; DOI=10.1128/JB.185.9.2759-2773.2003;
RA Chain P., Lamerdin J., Larimer F., Regala W., Land M., Hauser L.,
RA Hooper A., Klotz M., Norton J., Sayavedra-Soto L., Arciero D., Hommes N.,
RA Whittaker M., Arp D.;
RT "Complete genome sequence of the ammonia-oxidizing bacterium and obligate
RT chemolithoautotroph Nitrosomonas europaea.";
RL J. Bacteriol. 185:2759-2773(2003).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides. {ECO:0000256|RuleBase:RU363019}.
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|RuleBase:RU363019};
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000256|ARBA:ARBA00007365, ECO:0000256|RuleBase:RU363019}.
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DR EMBL; AL954747; CAD83953.1; -; Genomic_DNA.
DR AlphaFoldDB; Q82Y46; -.
DR STRING; 228410.NE0042; -.
DR KEGG; neu:NE0042; -.
DR eggNOG; COG0652; Bacteria.
DR HOGENOM; CLU_012062_16_9_4; -.
DR OrthoDB; 9807797at2; -.
DR PhylomeDB; Q82Y46; -.
DR Proteomes; UP000001416; Chromosome.
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; 2.40.100.10; Cyclophilin-like; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR044665; E_coli_cyclophilin_A-like.
DR PANTHER; PTHR43246; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE CYP38, CHLOROPLASTIC; 1.
DR PANTHER; PTHR43246:SF11; PEPTIDYLPROLYL ISOMERASE; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU363019};
KW Reference proteome {ECO:0000313|Proteomes:UP000001416};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|RuleBase:RU363019};
KW Signal {ECO:0000256|RuleBase:RU363019}.
FT SIGNAL 1..37
FT /evidence="ECO:0000256|RuleBase:RU363019"
FT CHAIN 38..213
FT /note="Peptidyl-prolyl cis-trans isomerase"
FT /evidence="ECO:0000256|RuleBase:RU363019"
FT /id="PRO_5006529320"
FT DOMAIN 46..203
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
SQ SEQUENCE 213 AA; 23372 MW; 13571A8B7C180E19 CRC64;
MKTFPFERQT ARPMKSITST GLFFILCLMI SATSAFAANP KVEIKTNLGA IQVELYPDQS
PKTVENFLNY VKDDYYTGTI FHRVIAGFMV QGGGFDQNYT QKPTRQPVEN EAANGLKNTI
GTIAMARTQD PHSASSQFFI NVANNHFLDY TAPTLQGYGY TVFGKVTSGM DVVNNIASSP
TGSNGPFNRD VPRKMIIIES IKLLPAAVSP ENP
//