ID A0A1Q3NMW9_9BACT Unreviewed; 223 AA.
AC A0A1Q3NMW9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU003915};
DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU003915};
GN ORFNames=BGO18_03150 {ECO:0000313|EMBL:OJU97146.1};
OS Candidatus Saccharibacteria bacterium 47-87.
OC Bacteria; Candidatus Saccharibacteria.
OX NCBI_TaxID=1895828 {ECO:0000313|EMBL:OJU97146.1, ECO:0000313|Proteomes:UP000185868};
RN [1] {ECO:0000313|EMBL:OJU97146.1, ECO:0000313|Proteomes:UP000185868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=47-87 {ECO:0000313|EMBL:OJU97146.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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, ECO:0000256|PROSITE-
CC ProRule:PRU00277, ECO:0000256|RuleBase:RU003915};
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family.
CC {ECO:0000256|ARBA:ARBA00006577, ECO:0000256|RuleBase:RU003915}.
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:OJU97146.1}.
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DR EMBL; MKSO01000001; OJU97146.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3NMW9; -.
DR STRING; 1895828.BGO18_03150; -.
DR Proteomes; UP000185868; 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 Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR PANTHER; PTHR43811:SF19; 39 KDA FK506-BINDING NUCLEAR PROTEIN; 1.
DR PANTHER; PTHR43811; FKBP-TYPE PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKPA; 1.
DR Pfam; PF00254; FKBP_C; 1.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277,
KW ECO:0000256|RuleBase:RU003915}; Membrane {ECO:0000256|SAM:Phobius};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|PROSITE-
KW ProRule:PRU00277}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 110..201
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
SQ SEQUENCE 223 AA; 23941 MW; B10B42D5A47435D5 CRC64;
MATTKVQRIG IWVIAAFMAV GTIGSFAIIV LANNNTQKDQ ARFNELYSKY QTEQSAYQAK
VDAQTKELSD KYFSTFSPYL SNVASFDASS VKELGKQDLV EGTGDAITSE SSFSAYYIGW
NPSGKMFDSS FSDAKDSLKA PLPVTPGGVI KGWTQGVDGM KVGGIRELTI PADLAYGKTG
SGADIPADTP LKFVVMIIPA PEAIAQPAMS SELITLYTRL YGK
//
