ID A0A0L6U3X0_9FIRM Unreviewed; 497 AA.
AC A0A0L6U3X0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|ARBA:ARBA00013194};
DE EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194};
GN ORFNames=AKG39_01805 {ECO:0000313|EMBL:KNZ43211.1};
OS Acetobacterium bakii.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Acetobacterium.
OX NCBI_TaxID=52689 {ECO:0000313|EMBL:KNZ43211.1, ECO:0000313|Proteomes:UP000036873};
RN [1] {ECO:0000313|Proteomes:UP000036873}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8239 {ECO:0000313|Proteomes:UP000036873};
RA Song Y., Hwang S., Cho B.-K.;
RT "Draft genome sequence of Acetobacterium bakii DSM 8293, a potential
RT psychrophilic chemical producer through syngas fermentation.";
RL Submitted (JUL-2015) 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};
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:KNZ43211.1}.
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DR EMBL; LGYO01000006; KNZ43211.1; -; Genomic_DNA.
DR RefSeq; WP_050738656.1; NZ_UOGO01000001.1.
DR AlphaFoldDB; A0A0L6U3X0; -.
DR STRING; 52689.AKG39_01805; -.
DR PATRIC; fig|52689.4.peg.3064; -.
DR OrthoDB; 14196at2; -.
DR Proteomes; UP000036873; 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 Gene3D; 1.10.4030.10; Porin chaperone SurA, peptide-binding domain; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR000297; PPIase_PpiC.
DR InterPro; IPR027304; Trigger_fact/SurA_dom_sf.
DR PANTHER; PTHR47245:SF1; FOLDASE PROTEIN PRSA; 1.
DR PANTHER; PTHR47245; PEPTIDYLPROLYL ISOMERASE; 1.
DR Pfam; PF13145; Rotamase_2; 1.
DR Pfam; PF13624; SurA_N_3; 2.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR SUPFAM; SSF109998; Triger factor/SurA peptide-binding domain-like; 2.
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:UP000036873};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 334..426
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 497 AA; 55406 MW; 55787A8D77BC7EA4 CRC64;
MKTKKLRTIT LLLAVTILIS FVGSGCSLVK VNPEADKKQV VAEINGEQIL KESYNNYLAY
YQMYYEASGM TFPTDVELKQ LQLDLLDDLV RVETMAAQGK KDGVTVDEAV LTADAESIIT
SIKTTLGDEK YAAALAKNNT DTGSFETFMK AFVANNEYAN TVAANYNSAL LLDPAKELTT
VVGTVGGDNV TKDVYNYRLS NEEFLAYYQN QEALATDDET MKTVNDNIFN TIAEQKAMTK
YAEENNLTLA QEDVDGYITS QQAFVNSLLP GDETLQQYLD GKYLTVAQYR EFEKQDAKAT
AAAAAIQADL ASKAKVSDKE IKTYYDENKN SYDTSTVSAK HILATDETLA KQIYEEAKNA
KTVEEFDAVM TKYQTVEGVS QATDLGAFTY ATMVSAFSDA AFGMEKNTVS EPVKTDYGYH
IIYVYDKNQA EIPALDTKKE EITEVLKNQK ATEEFDKLKT KLTKKLTIKF DKILTPLETY
MEQLKTDLNV EVFQNKI
//