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Database: UniProt
Entry: H5WZA5_9PSEU
LinkDB: H5WZA5_9PSEU
Original site: H5WZA5_9PSEU 
ID   H5WZA5_9PSEU            Unreviewed;       185 AA.
AC   H5WZA5;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 56.
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=SacmaDRAFT_0196 {ECO:0000313|EMBL:EHR48508.1};
OS   Saccharomonospora marina XMU15.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharomonospora.
OX   NCBI_TaxID=882083 {ECO:0000313|EMBL:EHR48508.1, ECO:0000313|Proteomes:UP000004926};
RN   [1] {ECO:0000313|EMBL:EHR48508.1, ECO:0000313|Proteomes:UP000004926}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XMU15 {ECO:0000313|EMBL:EHR48508.1,
RC   ECO:0000313|Proteomes:UP000004926};
RX   PubMed=22768369; DOI=10.4056/sigs.2655905;
RA   Klenk H.P., Lu M., Lucas S., Lapidus A., Copeland A., Pitluck S.,
RA   Goodwin L.A., Han C., Tapia R., Brambilla E.M., Potter G., Land M.,
RA   Ivanova N., Rohde M., Goker M., Detter J.C., Li W.J., Kyrpides N.C.,
RA   Woyke T.;
RT   "Genome sequence of the ocean sediment bacterium Saccharomonospora marina
RT   type strain (XMU15(T)).";
RL   Stand. Genomic Sci. 6:265-275(2012).
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}.
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DR   EMBL; CM001439; EHR48508.1; -; Genomic_DNA.
DR   RefSeq; WP_009151899.1; NZ_CM001439.1.
DR   AlphaFoldDB; H5WZA5; -.
DR   STRING; 882083.SacmaDRAFT_0196; -.
DR   eggNOG; COG0652; Bacteria.
DR   HOGENOM; CLU_012062_16_3_11; -.
DR   OrthoDB; 9807797at2; -.
DR   Proteomes; UP000004926; Chromosome.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   CDD; cd00317; cyclophilin; 1.
DR   Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR024936; Cyclophilin-type_PPIase.
DR   InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
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; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SUPFAM; SSF50891; Cyclophilin-like; 1.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|RuleBase:RU363019, ECO:0000313|EMBL:EHR48508.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004926};
KW   Rotamase {ECO:0000256|RuleBase:RU363019}.
FT   DOMAIN          21..182
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50072"
FT   BINDING         73..84
FT                   /ligand="cyclosporin A"
FT                   /ligand_id="ChEBI:CHEBI:4031"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001467-1"
FT   BINDING         89..90
FT                   /ligand="cyclosporin A"
FT                   /ligand_id="ChEBI:CHEBI:4031"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001467-1"
FT   BINDING         115..120
FT                   /ligand="cyclosporin A"
FT                   /ligand_id="ChEBI:CHEBI:4031"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001467-1"
FT   BINDING         125..129
FT                   /ligand="cyclosporin A"
FT                   /ligand_id="ChEBI:CHEBI:4031"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001467-1"
FT   BINDING         135
FT                   /ligand="cyclosporin A"
FT                   /ligand_id="ChEBI:CHEBI:4031"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001467-1"
FT   BINDING         141
FT                   /ligand="cyclosporin A"
FT                   /ligand_id="ChEBI:CHEBI:4031"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001467-1"
SQ   SEQUENCE   185 AA;  20133 MW;  564976952790E222 CRC64;
     MIRVTENNES LSGTKLKATL HTNRGDIRLN LFPDHAPKTV ANFTGLSEGT KEYTQPNAKG
     EKSGPFYDGS IFHRVIDGFM IQGGDPTGTG RGGPGYKFGD EFHPELQFNR PYLLAMANAG
     PGTNGSQFFI TVAPTPHLNF KHTIFGEVAD QESRDVVDEI ARTATGPADK PLEDIVIEQV
     SIERG
//
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