ID A0A0M2R3Z3_9PROT Unreviewed; 415 AA.
AC A0A0M2R3Z3;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Parvulin-like PPIase {ECO:0000256|ARBA:ARBA00018370};
DE AltName: Full=Peptidyl-prolyl cis-trans isomerase plp {ECO:0000256|ARBA:ARBA00030642};
DE AltName: Full=Rotamase plp {ECO:0000256|ARBA:ARBA00031484};
GN ORFNames=WH95_12420 {ECO:0000313|EMBL:KKJ76602.1};
OS Kiloniella litopenaei.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Kiloniellaceae; Kiloniella.
OX NCBI_TaxID=1549748 {ECO:0000313|EMBL:KKJ76602.1, ECO:0000313|Proteomes:UP000034491};
RN [1] {ECO:0000313|EMBL:KKJ76602.1, ECO:0000313|Proteomes:UP000034491}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1-1 {ECO:0000313|EMBL:KKJ76602.1,
RC ECO:0000313|Proteomes:UP000034491};
RA Shao Z., Wang L., Li X.;
RT "Genome sequence of Kiloniella sp. P1-1, isolated from the gut microflora
RT of Pacific white shrimp, Penaeus vannamei.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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:KKJ76602.1}.
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DR EMBL; LANI01000018; KKJ76602.1; -; Genomic_DNA.
DR RefSeq; WP_046507671.1; NZ_LANI01000018.1.
DR AlphaFoldDB; A0A0M2R3Z3; -.
DR STRING; 1549748.WH95_12420; -.
DR PATRIC; fig|1549748.8.peg.664; -.
DR OrthoDB; 9791746at2; -.
DR Proteomes; UP000034491; Unassembled WGS sequence.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-KW.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.40; -; 2.
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; IPR015391; SurA_N.
DR InterPro; IPR027304; Trigger_fact/SurA_dom_sf.
DR PANTHER; PTHR47637; CHAPERONE SURA; 1.
DR PANTHER; PTHR47637:SF1; CHAPERONE SURA; 1.
DR Pfam; PF00639; Rotamase; 1.
DR Pfam; PF09312; SurA_N; 1.
DR SUPFAM; SSF54534; FKBP-like; 2.
DR SUPFAM; SSF109998; Triger factor/SurA peptide-binding domain-like; 1.
DR PROSITE; PS50198; PPIC_PPIASE_2; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Reference proteome {ECO:0000313|Proteomes:UP000034491};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..415
FT /note="Parvulin-like PPIase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007021739"
FT DOMAIN 171..269
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 415 AA; 45498 MW; 770F09D647677A3C CRC64;
MRINFAANLL GFALMLTTAT TSFSQDVLRP AAVVNDDIIS LLDVSQRTQL AIVSSKQKNT
PQVRQRMVRQ VVRILIDERL KLQEAERLNI TISDQQVQRA LAAVAKQNKM TVQQLTDGLR
KQGVLQTTLL DQFRADIAWR AVVNRRLRSS VNISEAEIDE VITKLQSDGP AIQKRIFEIF
LGVDTASDEA KIKAQADEAL LTIRNGGNFS AIARQISQSN SAGLGGDLGW LQTGQLSNEL
QSAVESASAG SLLGPIRTKS GYYILLVQDQ RSAESEKKVR LKQFFFSLPA APSFEDTQKA
QSRAADARRK FTSCGEMDQL ADELGDEGSG DLGTVRTKDL PATTRSAIEQ VSVGQTTPAI
KVSGGLAVIA VCERQESGGV DRLAIQEKLT NDRLDTLARR YLLDLRRSSN VDIRL
//
