ID A0A0K2X3R7_9HELI Unreviewed; 162 AA.
AC A0A0K2X3R7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=HAL011_02230 {ECO:0000313|EMBL:CRF40466.1}, HAL013_16760
GN {ECO:0000313|EMBL:CRF43439.1}, HAL07_09840
GN {ECO:0000313|EMBL:CRF52519.1}, HAL09_05560
GN {ECO:0000313|EMBL:CRF43992.1};
OS Helicobacter ailurogastricus.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1578720 {ECO:0000313|EMBL:CRF40466.1, ECO:0000313|Proteomes:UP000038622};
RN [1] {ECO:0000313|EMBL:CRF40466.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ASB11 {ECO:0000313|EMBL:CRF40466.1}, ASB13
RC {ECO:0000313|EMBL:CRF43439.1}, ASB7 {ECO:0000313|EMBL:CRF52519.1}, and
RC ASB9 {ECO:0000313|EMBL:CRF43992.1};
RA Misic A.M., Cain C., Morris D.O., Rankin S., Beiting D.;
RT "Whole genome sequences of four Staphylococcus schleiferi canine
RT isolates.";
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000038622, ECO:0000313|Proteomes:UP000041394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Jaenicke S.;
RL Submitted (DEC-2014) 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}.
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DR EMBL; CDML01000006; CRF40466.1; -; Genomic_DNA.
DR EMBL; CDMH01000068; CRF43439.1; -; Genomic_DNA.
DR EMBL; CDMN01000021; CRF43992.1; -; Genomic_DNA.
DR EMBL; CDMG01000006; CRF52519.1; -; Genomic_DNA.
DR RefSeq; WP_053941988.1; NZ_FZMH01000001.1.
DR AlphaFoldDB; A0A0K2X3R7; -.
DR STRING; 1578720.HAL011_02230; -.
DR GeneID; 82131944; -.
DR OrthoDB; 9807797at2; -.
DR Proteomes; UP000038622; Unassembled WGS sequence.
DR Proteomes; UP000041394; Unassembled WGS sequence.
DR Proteomes; UP000043437; Unassembled WGS sequence.
DR Proteomes; UP000045175; 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:CRF40466.1};
KW Rotamase {ECO:0000256|RuleBase:RU363019}.
FT DOMAIN 16..149
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
SQ SEQUENCE 162 AA; 17475 MW; 6309404AB18DFB57 CRC64;
MKPLKVFETS PEALKSYHTA TIQTSKGAIK VHLFGEDAPQ AVTNFATLAK EGFYNGLNFH
RVIAGFVAQG GCPLGTGMGG PEYRIKCEVA NNPHKHERGA MSMAHAGRDT GGSQFFLCFT
PQPHLDGEHT VFGQIEDEAS LQVLDSLKQG DKIESIQISA QS
//
