ID A0A252DAM7_9NOSO Unreviewed; 267 AA.
AC A0A252DAM7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=BV372_28855 {ECO:0000313|EMBL:OUL24621.1};
OS Nostoc sp. T09.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=1932621 {ECO:0000313|EMBL:OUL24621.1, ECO:0000313|Proteomes:UP000195076};
RN [1] {ECO:0000313|EMBL:OUL24621.1, ECO:0000313|Proteomes:UP000195076}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T09 {ECO:0000313|EMBL:OUL24621.1};
RA Cruz-Morales P., Corona-Gomez J.A., Gutierrez-Garcia K.G., Barona-Gomez F.,
RA Cibrian-Jaramillo A.;
RT "Metagenomics of subcommunity co-cultures reveals the complexity of the
RT cycad coralloid root endophytic microbiome.";
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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:OUL24621.1}.
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DR EMBL; MTAV01000169; OUL24621.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A252DAM7; -.
DR OrthoDB; 9796864at2; -.
DR Proteomes; UP000195076; 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; 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; PS50072; CSA_PPIASE_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU363019};
KW Reference proteome {ECO:0000313|Proteomes:UP000195076};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|RuleBase:RU363019};
KW Signal {ECO:0000256|RuleBase:RU363019}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|RuleBase:RU363019"
FT CHAIN 20..267
FT /note="Peptidyl-prolyl cis-trans isomerase"
FT /evidence="ECO:0000256|RuleBase:RU363019"
FT /id="PRO_5011811985"
FT DOMAIN 93..246
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT REGION 27..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 267 AA; 28135 MW; 5357D76A9FC80D29 CRC64;
MRLKFPQFLV ALVIVGALAL GGCSTQQDAS KASAPTSTAT STATSTATET SSKATTEATS
VSETTSESIP GMKDLPRLEG KATVVITVKG SPITVEVDGT NAPITAGNFV DLVQRGVYDG
TVFHRVVRDP QPFVVQGGDP QSKDPKVPVN RLGTGGFIDP KTKNERYIPL EIKPKGSEQL
VYGKTITQPP VLTHKLGAVA MARSQQPDSA SSQFYFALAD LGFLDGNYAV FGNVTEGFDV
VNKIQQGDRI DSAKVTKGAE NLKTSGQ
//
