ID   B1WNU2_CROS5            Unreviewed;       243 AA.
AC   B1WNU2;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   02-SEP-2026, entry version 90.
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=ppiB {ECO:0000313|EMBL:ACB51521.1};
GN   OrderedLocusNames=cce_2171 {ECO:0000313|EMBL:ACB51521.1};
OS   Crocosphaera subtropica (strain ATCC 51142 / BH68) (Cyanothece sp. (strain
OS   ATCC 51142)).
OC   Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Aphanothecaceae; Crocosphaera; Crocosphaera subtropica.
OX   NCBI_TaxID=43989 {ECO:0000313|EMBL:ACB51521.1, ECO:0000313|Proteomes:UP000001203};
RN   [1] {ECO:0000313|EMBL:ACB51521.1, ECO:0000313|Proteomes:UP000001203}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51142 / BH68 {ECO:0000313|Proteomes:UP000001203};
RX   PubMed=18812508; DOI=10.1073/pnas.0805418105;
RA   Welsh E.A., Liberton M., Stoeckel J., Loh T., Elvitigala T., Wang C.,
RA   Wollam A., Fulton R.S., Clifton S.W., Jacobs J.M., Aurora R., Ghosh B.K.,
RA   Sherman L.A., Smith R.D., Wilson R.K., Pakrasi H.B.;
RT   "The genome of Cyanothece 51142, a unicellular diazotrophic cyanobacterium
RT   important in the marine nitrogen cycle.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:15094-15099(2008).
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|RuleBase:RU363019}.
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DR   EMBL; CP000806; ACB51521.1; -; Genomic_DNA.
DR   RefSeq; WP_009546922.1; NC_010546.1.
DR   AlphaFoldDB; B1WNU2; -.
DR   STRING; 43989.cce_2171; -.
DR   KEGG; cyt:cce_2171; -.
DR   eggNOG; COG0652; Bacteria.
DR   HOGENOM; CLU_012062_16_4_3; -.
DR   OrthoDB; 9796864at2; -.
DR   Proteomes; UP000001203; Chromosome circular.
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   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|PROSITE-
KW   ProRule:PRU00156}; Lipoprotein {ECO:0000256|PROSITE-ProRule:PRU00303};
KW   Palmitate {ECO:0000256|PROSITE-ProRule:PRU00303};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001203};
KW   Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|PROSITE-
KW   ProRule:PRU00156};
KW   Signal {ECO:0000256|PROSITE-ProRule:PRU00303,
KW   ECO:0000256|RuleBase:RU363019}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|RuleBase:RU363019"
FT   CHAIN           26..243
FT                   /note="Peptidyl-prolyl cis-trans isomerase"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00303"
FT                   /id="PRO_5049680736"
FT   CHAIN           30..243
FT                   /note="Peptidyl-prolyl cis-trans isomerase"
FT                   /evidence="ECO:0000256|RuleBase:RU363019"
FT                   /id="PRO_5006522166"
FT   DOMAIN          72..225
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50072"
FT   LIPID           26
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00303"
FT   LIPID           26
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   243 AA;  26330 MW;  44468FE646A2BB08 CRC64;
     MRNLKKRWLT TLACLILVSG LMITGCSNAS NNSETAVNPN ENQQVSQLNM DNYVPRLEGN
     AVVEMTINGS PVTIEVKGDD APITAGNFVD LVERGFYNGL TFHRVVKDPQ PFVAQGGDPQ
     GTGMGGFVDP ETKQERRIPL EIKLEGDEKP TYSKALGQQG NRTAMSQPVV LDHERGAVAM
     ARSGMPDSAS SQFYFALSDL EFLNGDYAVF GKVTEGMDVV DGIKQGDRID SAKVVSGLEN
     LKQ
//