ID Q2IHN5_ANADE Unreviewed; 356 AA.
AC Q2IHN5;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE SubName: Full=PpiC-type peptidyl-prolyl cis-trans isomerase {ECO:0000313|EMBL:ABC84096.1};
GN OrderedLocusNames=Adeh_4333 {ECO:0000313|EMBL:ABC84096.1};
OS Anaeromyxobacter dehalogenans (strain 2CP-C).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Anaeromyxobacteraceae; Anaeromyxobacter.
OX NCBI_TaxID=290397 {ECO:0000313|EMBL:ABC84096.1, ECO:0000313|Proteomes:UP000001935};
RN [1] {ECO:0000313|Proteomes:UP000001935}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2CP-C {ECO:0000313|Proteomes:UP000001935};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R.,
RA Gilna P., Kiss H., Schmutz J., Larimer F., Land M., Kyrpides N.,
RA Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R.,
RA Zhulin I.B., Loeffler F.E., Richardson P.;
RT "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000251; ABC84096.1; -; Genomic_DNA.
DR RefSeq; WP_011423378.1; NC_007760.1.
DR AlphaFoldDB; Q2IHN5; -.
DR STRING; 290397.Adeh_4333; -.
DR KEGG; ade:Adeh_4333; -.
DR eggNOG; COG0760; Bacteria.
DR HOGENOM; CLU_034646_5_3_7; -.
DR OrthoDB; 5380974at2; -.
DR Proteomes; UP000001935; Chromosome.
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 SUPFAM; SSF54534; FKBP-like; 1.
DR SUPFAM; SSF109998; Triger factor/SurA peptide-binding domain-like; 1.
DR PROSITE; PS50198; PPIC_PPIASE_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW ECO:0000313|EMBL:ABC84096.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001935};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..356
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007923164"
FT DOMAIN 141..250
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
FT REGION 317..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..356
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 356 AA; 38359 MW; B51000A6F7CE8BA4 CRC64;
MLRRIALLGL VALAATACQP QSKDSKKSGP AVATGNGFTI TAGELKARLD EQSPFIRARY
STLERKKEFL DNLVRFEVLA REAERQGLAN DPEVQLTLKK VMVQKLVQKN FQDASGAAAE
ALPEADLQKY YDEHKAEYYR PRRVRLAAIV WNAPAGSPER AAKVALAKKA LAKLKAEEKK
NTLAFAQLVN EFSEDAASKA TAGDLGFKTR EDLEKAYSKE FADVAYNLQP GATSGVLETP
NGVYLVKGTG EQDELNRTFE QVKPQIQTKL YREKKTKEFD AWLKKLRDDA KVSIDEKALE
AVEVSAAAPA GMGGMPGMPG MMPGGHGPMG AGPRPMGAPA PAAAPAQPAP APAPAK
//
