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Database: UniProt
Entry: K9QCH1_9NOSO
LinkDB: K9QCH1_9NOSO
Original site: K9QCH1_9NOSO 
ID   K9QCH1_9NOSO            Unreviewed;       263 AA.
AC   K9QCH1;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 55.
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=Nos7107_2462 {ECO:0000313|EMBL:AFY43068.1};
OS   Nostoc sp. PCC 7107.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=317936 {ECO:0000313|EMBL:AFY43068.1, ECO:0000313|Proteomes:UP000010381};
RN   [1] {ECO:0000313|EMBL:AFY43068.1, ECO:0000313|Proteomes:UP000010381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7107 {ECO:0000313|EMBL:AFY43068.1,
RC   ECO:0000313|Proteomes:UP000010381};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA   Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA   Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA   Pitluck S., Woyke T., Kerfeld C.;
RT   "Finished genome of Nostoc sp. PCC 7107.";
RL   Submitted (AUG-2012) 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}.
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DR   EMBL; CP003548; AFY43068.1; -; Genomic_DNA.
DR   RefSeq; WP_015113283.1; NC_019676.1.
DR   AlphaFoldDB; K9QCH1; -.
DR   STRING; 317936.Nos7107_2462; -.
DR   KEGG; nos:Nos7107_2462; -.
DR   PATRIC; fig|317936.3.peg.2668; -.
DR   eggNOG; COG0652; Bacteria.
DR   HOGENOM; CLU_012062_16_4_3; -.
DR   InParanoid; K9QCH1; -.
DR   OrthoDB; 9796864at2; -.
DR   Proteomes; UP000010381; Chromosome.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd01924; cyclophilin_TLP40_like; 1.
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:UP000010381};
KW   Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|RuleBase:RU363019};
KW   Signal {ECO:0000256|RuleBase:RU363019}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|RuleBase:RU363019"
FT   CHAIN           29..263
FT                   /note="Peptidyl-prolyl cis-trans isomerase"
FT                   /evidence="ECO:0000256|RuleBase:RU363019"
FT                   /id="PRO_5006527623"
FT   DOMAIN          85..263
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50072"
FT   REGION          28..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          125..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..64
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   263 AA;  27998 MW;  5D5920EE3AE3B974 CRC64;
     MRLKVTKFLV TFLMVAALML GGCSTQQVGS NSSSPATASQ TSTTTTTAEA TSVSETTSES
     IPGMNNLPRL EGKATVVMTV NGKPITIEVD GTNAPITAGN FVDLVQKGVY DGLAFHRVVR
     DPQPFVVQGG DPQGKDPKFP ASRLGTGGYI DPKTGNERYI PLEIKPKGEA SPIYSKTFEM
     ARVTTTPELT HKQGAIAMAR SQQPDSASSQ FYFALADLGF LDGNYAVFGQ VTQGFDVVNK
     IQQGDRIESA KVTQGAENLK VPQ
//
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