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Database: UniProt
Entry: M1YZ17_NITG3
LinkDB: M1YZ17_NITG3
Original site: M1YZ17_NITG3 
ID   M1YZ17_NITG3            Unreviewed;       184 AA.
AC   M1YZ17;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 52.
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=NITGR_360050 {ECO:0000313|EMBL:CCQ90712.1};
OS   Nitrospina gracilis (strain 3/211).
OC   Bacteria; Nitrospinae/Tectomicrobia group; Nitrospinota; Nitrospinia;
OC   Nitrospinales; Nitrospinaceae; Nitrospina.
OX   NCBI_TaxID=1266370 {ECO:0000313|EMBL:CCQ90712.1, ECO:0000313|Proteomes:UP000011704};
RN   [1] {ECO:0000313|EMBL:CCQ90712.1, ECO:0000313|Proteomes:UP000011704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3/211 {ECO:0000313|EMBL:CCQ90712.1,
RC   ECO:0000313|Proteomes:UP000011704};
RX   PubMed=23439773; DOI=10.3389/fmicb.2013.00027;
RA   Luecker S., Nowka B., Rattei T., Spieck E., and Daims H.;
RT   "The genome of Nitrospina gracilis illuminates the metabolism and evolution
RT   of the major marine nitrite oxidizer.";
RL   Front. Microbiol. 4:27-27(2013).
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:CCQ90712.1}.
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DR   EMBL; CAQJ01000040; CCQ90712.1; -; Genomic_DNA.
DR   AlphaFoldDB; M1YZ17; -.
DR   STRING; 1266370.NITGR_360050; -.
DR   HOGENOM; CLU_012062_16_0_0; -.
DR   InParanoid; M1YZ17; -.
DR   OMA; ELYNDHA; -.
DR   Proteomes; UP000011704; 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:CCQ90712.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011704};
KW   Rotamase {ECO:0000256|RuleBase:RU363019}.
FT   DOMAIN          24..176
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50072"
SQ   SEQUENCE   184 AA;  20778 MW;  A6C2E019A7A3FB37 CRC64;
     MHNLIRVVFI TIFMAWGISS TVWAGEIAVI QTKFGNMKIE FFEDQAPGHV KNFKDLAKKG
     FYDGTLFHRV IPGFMIQGGD PNTRNQQREM HGMGGPGYTI DAEFSNIPHD RGIVSMARAQ
     DPNSAGSQFF IVVKDAHFLD KKYTVFGRVT EGMEVADKIV SQRRDHNDNP FDPIAMKVII
     KKDK
//
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