GenomeNet

Database: UniProt
Entry: A0A0R1ZRP9_9LACO
LinkDB: A0A0R1ZRP9_9LACO
Original site: A0A0R1ZRP9_9LACO 
ID   A0A0R1ZRP9_9LACO        Unreviewed;       194 AA.
AC   A0A0R1ZRP9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
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   ORFNames=FC18_GL000564 {ECO:0000313|EMBL:KRM54345.1};
OS   Lacticaseibacillus sharpeae JCM 1186 = DSM 20505.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lacticaseibacillus.
OX   NCBI_TaxID=1291052 {ECO:0000313|EMBL:KRM54345.1, ECO:0000313|Proteomes:UP000051679};
RN   [1] {ECO:0000313|EMBL:KRM54345.1, ECO:0000313|Proteomes:UP000051679}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20505 {ECO:0000313|EMBL:KRM54345.1,
RC   ECO:0000313|Proteomes:UP000051679};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
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|ARBA:ARBA00002388,
CC       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}.
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:KRM54345.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AYYO01000056; KRM54345.1; -; Genomic_DNA.
DR   RefSeq; WP_054675806.1; NZ_BBAC01000001.1.
DR   AlphaFoldDB; A0A0R1ZRP9; -.
DR   STRING; 1291052.FC18_GL000564; -.
DR   PATRIC; fig|1291052.5.peg.575; -.
DR   OrthoDB; 9807797at2; -.
DR   Proteomes; UP000051679; Unassembled WGS sequence.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR024936; Cyclophilin-type_PPIase.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   InterPro; IPR044666; Cyclophilin_A-like.
DR   PANTHER; PTHR45625; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE-RELATED; 1.
DR   PANTHER; PTHR45625:SF4; PEPTIDYLPROLYL ISOMERASE DOMAIN AND WD REPEAT-CONTAINING PROTEIN 1; 1.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   PIRSF; PIRSF001467; Peptidylpro_ismrse; 2.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SUPFAM; SSF50891; Cyclophilin-like; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|RuleBase:RU363019, ECO:0000313|EMBL:KRM54345.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051679};
KW   Rotamase {ECO:0000256|RuleBase:RU363019}.
FT   DOMAIN          19..192
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50072"
SQ   SEQUENCE   194 AA;  20871 MW;  BBB2161836411B53 CRC64;
     MTYPQLDLAN HQGPTVTLNT NHGDIVIALF PDVAPKTVAN FVGLTKKGYY DGIIFHRVIP
     DFMIQGGDPT GTGMGGESIY GDSFEDEFSN QAFNLRGALS MANAGPNTNG SQFFIVQNKN
     INNGFLQQMD AAGYPAEIIE AYKQGGTPWL DHRHTVFGQV MTGMDVVDEI AGVKTLPGDK
     PAEDVTIISA TVTE
//
DBGET integrated database retrieval system