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Database: UniProt
Entry: A0A0H3E0R5_BACA1
LinkDB: A0A0H3E0R5_BACA1
Original site: A0A0H3E0R5_BACA1 
ID   A0A0H3E0R5_BACA1        Unreviewed;       146 AA.
AC   A0A0H3E0R5;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, entry version 38.
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   OrderedLocusNames=BATR1942_09585 {ECO:0000313|EMBL:ADP32850.1};
OS   Bacillus atrophaeus (strain 1942).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=720555 {ECO:0000313|EMBL:ADP32850.1, ECO:0000313|Proteomes:UP000006867};
RN   [1] {ECO:0000313|Proteomes:UP000006867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1942 {ECO:0000313|Proteomes:UP000006867};
RA   Gibbons H.S., Broomall S., McNew L.A., Daligault H., Chapman C., Bruce D.,
RA   Karavis M., McGregor P., Hong C., Park K.H., Akmal A., Feldman A.,
RA   Lin J.S., Chang W.E., Higgs B.W., Demirev P., Lindquist J., Liem A.,
RA   Fochler E., Tapia R., Bishop-Lilly K., Detter C., Han C., Sozhamannan S.,
RA   Rosenzweig C.N., Skowronski E.;
RT   "Genomic signatures of strain selection and enhancement in Bacillus
RT   atrophaeus subsp. Globigii, a historical biowarfare simulant.";
RL   Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADP32850.1, ECO:0000313|Proteomes:UP000006867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1942 {ECO:0000313|EMBL:ADP32850.1,
RC   ECO:0000313|Proteomes:UP000006867};
RX   PubMed=21464989; DOI=10.1371/journal.pone.0017836;
RA   Gibbons H.S., Broomall S.M., McNew L.A., Daligault H., Chapman C.,
RA   Bruce D., Karavis M., Krepps M., McGregor P.A., Hong C., Park K.H.,
RA   Akmal A., Feldman A., Lin J.S., Chang W.E., Higgs B.W., Demirev P.,
RA   Lindquist J., Liem A., Fochler E., Read T.D., Tapia R., Johnson S.,
RA   Bishop-Lilly K.A., Detter C., Han C., Sozhamannan S., Rosenzweig C.N.,
RA   Skowronski E.W.;
RT   "Genomic signatures of strain selection and enhancement in Bacillus
RT   atrophaeus var. globigii, a historical biowarfare simulant.";
RL   PLoS ONE 6:E17836-E17836(2011).
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|ARBA:ARBA00000971,
CC         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; CP002207; ADP32850.1; -; Genomic_DNA.
DR   RefSeq; WP_004429645.1; NC_014639.1.
DR   AlphaFoldDB; A0A0H3E0R5; -.
DR   GeneID; 23410372; -.
DR   KEGG; bae:BATR1942_09585; -.
DR   eggNOG; COG0652; Bacteria.
DR   HOGENOM; CLU_012062_16_4_9; -.
DR   OMA; ELYNDHA; -.
DR   OrthoDB; 9807797at2; -.
DR   Proteomes; UP000006867; 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};
KW   Rotamase {ECO:0000256|RuleBase:RU363019}.
FT   DOMAIN          14..146
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50072"
SQ   SEQUENCE   146 AA;  15677 MW;  EA010EC65FCD2491 CRC64;
     MAKKGYILME NGEKIEFDLF PNEAPNTVAN FENLANTGFY DGVTFHRVIP GFVSQGGDPT
     GTGMGGSEKT IKCETEGNPH KHEAGSLSMA HAGKDTGSSQ FFIVHEPQPH LNGVHTVFGK
     VTSGLETARS MSNGDTMKEV KVFDAE
//
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