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}.
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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
//