ID A0A1V4EBJ6_9ACTN Unreviewed; 282 AA.
AC A0A1V4EBJ6;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=B1L11_23985 {ECO:0000313|EMBL:OPG10256.1};
OS Microbispora sp. GKU 823.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Microbispora.
OX NCBI_TaxID=1652100 {ECO:0000313|EMBL:OPG10256.1, ECO:0000313|Proteomes:UP000190255};
RN [1] {ECO:0000313|EMBL:OPG10256.1, ECO:0000313|Proteomes:UP000190255}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GKU 823 {ECO:0000313|EMBL:OPG10256.1,
RC ECO:0000313|Proteomes:UP000190255};
RA Kruasuwan W.;
RT "Draft genome sequence of sugarcane root-associated plant growth promoting
RT Microbispora sp. GKU 823.";
RL Submitted (FEB-2017) 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|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:OPG10256.1}.
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DR EMBL; MWJN01000046; OPG10256.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4EBJ6; -.
DR OrthoDB; 5507614at2; -.
DR Proteomes; UP000190255; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR CDD; cd00317; cyclophilin; 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; IPR044666; Cyclophilin_A-like.
DR PANTHER; PTHR45625:SF3; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE B-RELATED; 1.
DR PANTHER; PTHR45625; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE-RELATED; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|RuleBase:RU363019, ECO:0000313|EMBL:OPG10256.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Rotamase {ECO:0000256|RuleBase:RU363019};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 33..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 122..278
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT REGION 59..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 282 AA; 29484 MW; 874927969D1A7648 CRC64;
MVTGKDRQKQ LAREHYERQL RARAEREQKS RRTAIIGTTA AVVVVIGGVV AATTLLGRDD
SSATASASPS ASIKPAVADP KPYDPAKGTC GYVADEGSGQ VKNVGMPPEK VSTAPATMTI
KTNLGDIVAR LDSEKAPCTV NSFKFLASKD YFDNTKCHRM GTDFPILQCG DPLAKADGKN
PTDGQGGPGY RFANENLAGA KYTRGVIAMA NSGPNTNGSQ FFIVFGDTGL TPDYTPFGTV
TKGLEIVDKV AKKGVIPSAG GDGTGAPKQP VVIKDVTITS KS
//
