ID A0A1J6WTD2_9BACI Unreviewed; 145 AA.
AC A0A1J6WTD2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=BHE18_10705 {ECO:0000313|EMBL:OIU71475.1};
OS Rossellomorea aquimaris.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Rossellomorea.
OX NCBI_TaxID=189382 {ECO:0000313|EMBL:OIU71475.1, ECO:0000313|Proteomes:UP000182062};
RN [1] {ECO:0000313|EMBL:OIU71475.1, ECO:0000313|Proteomes:UP000182062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAMM {ECO:0000313|EMBL:OIU71475.1,
RC ECO:0000313|Proteomes:UP000182062};
RA Waghmode S.R., Suryavanshi M.V.;
RT "Bacillus aquimaris SAMM genome sequence reveals colonization and
RT biosurfactant production capacities.";
RL Submitted (SEP-2016) 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|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}.
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:OIU71475.1}.
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DR EMBL; MINN01000085; OIU71475.1; -; Genomic_DNA.
DR RefSeq; WP_071618861.1; NZ_MINN01000085.1.
DR AlphaFoldDB; A0A1J6WTD2; -.
DR OrthoDB; 9807797at2; -.
DR Proteomes; UP000182062; Unassembled WGS sequence.
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:OIU71475.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000182062};
KW Rotamase {ECO:0000256|RuleBase:RU363019}.
FT DOMAIN 14..145
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
SQ SEQUENCE 145 AA; 15692 MW; B07F2AE2E95E8F07 CRC64;
MAKKGYIQFQ TGEKVEFDLF PNEAPGTVEN FEKLAKEGFY DGLTFHRVIP GFVSQGGCPN
GNGMGGPGYT IKCETEGNPH KHEEGSLSMA HAGKDTGGSQ FFIVHEPQPH LNGVHTVFGK
VTSGIDTVKS MRNGDVMEKV EVFDA
//