ID A0A1H9THC6_9BACI Unreviewed; 317 AA.
AC A0A1H9THC6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|ARBA:ARBA00013194};
DE EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194};
GN ORFNames=SAMN05444126_11018 {ECO:0000313|EMBL:SER96437.1};
OS Salisediminibacterium haloalkalitolerans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Salisediminibacterium.
OX NCBI_TaxID=1464123 {ECO:0000313|EMBL:SER96437.1, ECO:0000313|Proteomes:UP000199318};
RN [1] {ECO:0000313|EMBL:SER96437.1, ECO:0000313|Proteomes:UP000199318}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10nlg {ECO:0000313|EMBL:SER96437.1,
RC ECO:0000313|Proteomes:UP000199318};
RA de Groot N.N.;
RL Submitted (OCT-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};
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DR EMBL; FOGV01000010; SER96437.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9THC6; -.
DR STRING; 1464123.SAMN05444126_11018; -.
DR Proteomes; UP000199318; Unassembled WGS sequence.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR000297; PPIase_PpiC.
DR InterPro; IPR023058; PPIase_PpiC_CS.
DR InterPro; IPR027304; Trigger_fact/SurA_dom_sf.
DR PANTHER; PTHR47245:SF1; FOLDASE PROTEIN PRSA; 1.
DR PANTHER; PTHR47245; PEPTIDYLPROLYL ISOMERASE; 1.
DR Pfam; PF13616; Rotamase_3; 1.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR SUPFAM; SSF109998; Triger factor/SurA peptide-binding domain-like; 1.
DR PROSITE; PS01096; PPIC_PPIASE_1; 1.
DR PROSITE; PS50198; PPIC_PPIASE_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|PROSITE-
KW ProRule:PRU00278}; Reference proteome {ECO:0000313|Proteomes:UP000199318};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..317
FT /note="peptidylprolyl isomerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038879384"
FT DOMAIN 174..265
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
FT REGION 25..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 317 AA; 36376 MW; 7B41A1C29491F267 CRC64;
MKKLMYTLAI SSLFLFACSA ANDEQEEENS ETNNAVSQES NDYNGNERED PTLNGDNLVV
ESEAGTISKD DFYEELKASH GEAVLNRLIE KMIIEAEAEN LGIDDETVQA EMEQLMENYG
ADNETEFYEL FTRQDAEDED DMEHLIKRQL VMEEYTDNME RITEDALETE YERGRMVEAR
HILVSDQEEA DELYRRLTED QASFADLAAE YSTDPTSSDD GGNVGSFQRG TMNPAFERTA
FLLDVGEISE PVKGPSGYHI IEVTDRTDFD EPFAEVREQL RTTLEDRRLY MMTEQQGELF
DSYDIDIHDD ELDHLFP
//
